A Proteomics Perspective From Animal Welfare To Food Safety

Send Orders for Reprints to reprints@benthamscience.
net
156 Current Protein and Peptide Science, 2014, 15, 156-168
A Proteomics Perspective: From Animal Welfare to Food Safety
Anna Bassols
1
, Romana Turk
2
and Paola Roncada
3,4,*

1
Departament de Bioqumica i Biologia Molecular, Facultat de Veterinria, Universitat Autnoma de Barcelona Cer-
danyola del Valls, Barcelona, Spain;
2
Faculty of Veterinary Medicine, University of Zagreb, Department of Patho-
physiology, Zagreb, Croatia;
3
Istituto Sperimentale Italiano Lazzaro Spallanzani, Milano;
4
Dipartimento di Scienze
Veterinarie e Sanit Pubblica, Universit degli Studi di Milano, Via Celoria 10, 20133 Milano, Italy
Abstract: A fundamental issue of farm animal welfare is to keep animals clinically healthy, without disease or stress, par-
ticularly in intensive breeding, in order to produce safe and quality food. This issue is highly relevant for the food industry
worldwide as they are directly linked to public health and welfare. The aim of this review is to explore how proteomics
can assess and improve the knowledge useful for the strategic management of products of animal origin. Useful indica-
tions are provided about the latest proteomics tools for the development of novel biotechnologies serving the public
health. The multivariate proteomics approach provides the bases for the discovery of biomarkers useful to investigate ad-
aptation syndromes and oxidative stress. These two responses represent the milestones for the study of animal welfare.
Moreover their implementation in the characterization and standardization of raw materials, process development, and
quality and safety control of the final product of animal origin represents the current frontier in official surveillance and
tests development.
Keywords: Animal welfare, foodborne pathogens, food safety, immunoresponse, proteomics, stress.
1. INTRODUCTION
Animal welfare is a hallmark to assess food quality and
safety. The safety of food chain is indirectly influenced by
animal welfare. This is given by the strict link that occurs
between animal welfare, animal health and foodborne patho-
gens. Stress factors and the lack of healthy conditions for
animal welfare may lead animals to increase their suscepti-
bility to diseases. This could represent a serious issue for
consumers who may in turn be exposed to common food
borne pathogens such as Salmonella, Campylobacter and E.
coli. If the general management of a breeder is correct under
hygienic conditions, the key point influencing animal wel-
fare is stress. Proteomics represents an innovative biotechno-
logical approach to act and investigate at different levels of
the food chain. The implementation of the new biotechno-
logical tools derived from proteomics represents an impor-
tant challenge for the development of responsible biotech-
nology serving the public health by providing advanced ana-
lytical methods. The aim of this review is to provide the fun-
damental concepts of the potential application of proteomics
in different areas of food quality and safety. In particular the
power of proteomic tools to investigate how animal welfare
can influence food production will be highlighted.
Proteomics offers the possibility of a global overview of
the whole organism adaptation response to stress conditions
and provides information on biomarkers that may be signifi-
cant indicators of animal welfare based on a molecular

*Address correspondence to this author at the Dipartimento di Scienze Vet-
erinarie e Sanit Pubblica, Universit degli Studi di Milano, Via Celoria 10,
20133 Milano, Italy; Tel: +390250318138;
E-mails: paola.roncada@guest.unimi.it and paola.roncada@gmail.com
analytical response. Proteins are major targets for stress-
associated post-translational modifications, such as oxida-
tion, given their high overall abundance in biological sys-
tems and because they are primarily responsible for most
functional processes within the cells. In a condition of in-
creased oxidative status of the organism, a proteomic ap-
proach allows to detect and identify changes in the concen-
tration of enzymes involved in redox metabolism as well as
in the level of oxidised proteins. Oxidative modifications in
the protein structure can provide a typical fingerprint such as
carbonylation of amino acids, detectable through proteomic
tools [1-3]. Farm animals are subjected to physiological,
pathological and environmental conditions that can affect
health as well as characteristics of the final product (meat,
milk, etc.) and safety issues and food quality aspects (meat
tenderness, protein composition, etc.). Since animals are
many times bred in crowded farms, this leads to a highly
challenging and adverse environment and, sometimes, to
multiple risks for the onset of infectious diseases with a high
risk of propagation. Problems concerning welfare could be
due to excessive crowding of the animals, but also to mixing
of the animals leading to a disruption of their hierarchical
social structures (specially with pigs), transport to the
slaughterhouse in long and uncomfortable travels, etc [4, 5].
Furthermore, the genetic selection in the direction of im-
proved food quantity and quality produced extreme pheno-
types with increasing health problems (for example, high
incidence of bovine mastitis associated to extreme milk
yields, or colostrum deprivation in hyperprolific sows). Both
intensive animal production and genetic selection results in
an overall decrease of animal welfare. For this reason it is
more and more necessary to know the mechanisms of patho-
genesis of the most frequently occurring diseases in farm
1875-5550/14 $58.00+.00 2014 Bentham Science Publishers
A Proteomics Perspective: From Animal Welfare to Food Safety Current Protein and Peptide Science, 2014, Vol. 15, No. 2 157
animals to control welfare and safety issues. In this context,
proteomics has an important role for the discovery of bio-
markers to monitor health and welfare and in the study of
diseases and the production of new vaccines [6-8]. The over-
all final aim is to optimize a sustainable equilibrium between
productivity, product quality and animal welfare.

Fig. (1). Factors that can direcly or indirectly influence food safety.

Fig. (2). How proteomics can act at different levels from farm to
fork.

2. STRESS AND ITS IMPACT ON FARM ANIMAL
WELFARE
Different stressors, such as transport, housing and tem-
perature conditions, feed deprivation before slaughtering,
physiological conditions like pregnancy and lactation, patho-
gens etc. can trigger a nonspecific response needed to re-
establish homeostasis of the body. Moreover, during space
allocation, animals are exposed to a wide range of stimuli,
including increased human contact, vibration during trans-
port, unknown environments and food and water deprivation.
Stress is defined as the unspecific response of the body to
different exogenous or external adverse environment [9].
The stress response provokes a range of modifications usu-
ally called general adaptation syndrome. Moreover, chronic
stress may result in pathological states and lead to distur-
bances of health, growth and fertility thus impairing the effi-
ciency of animal production[10]. Chronic stress, in particu-
lar, suppresses the immune system and increases the suscep-
tibility to infections, pathogen shedding, and carcass con-
tamination [11].
Welfare problems may cause great economic losses and
are important for ethical reasons and public opinion. In this
context, there is an increasing interest in the measurement of
stress as an indicator of animal welfare, nutritional status and
disease. Behavioral and physiological markers are commonly
used, but they may increase by other causes [12, 13]. Indica-
tors of nutritional stress include mainly non-esterified fatty
acids (NEFAs) and 3-hydroxybutyrate. Acute phase proteins
(APPs), such as Pig-MAP and haptoglobin, are recognized
markers of inflammation [14, 15] and have also been pro-
posed as indicators of stress in cattle and pigs [16, 17]. Nev-
ertheless, objective laboratorial criteria to evaluate animal
stress are still lacking and proteomics may be useful to
achieve this goal.
2.1. Impact of Stress on Farm Animal Production
Stress results in the release of a number of different hor-
mones, neurotransmitters, cytokines and other factors into
the circulation or tissues. Particularly, increased levels of
glucocorticoids inhibit growth hormone (GH) secretion from
pituitary gland inhibiting the animal growth during stress
response [18]. Stress can also have a harmful effect on the
quality of food products of farm animals (meat, milk and
eggs). Growth performance and product quality are com-
promised in cows and small ruminants (sheep and goats) and
also in pigs due to different stressors such as space allocation
and heat stress [19-22]. In addition, cold stress in swine has
been recognized as a cause of neonatal morbidity and mortal-
ity [23]. There are experimental evidences that show how
environmental stress in breeding can cause problems in ani-
mal fertility [24]. In particular heat is a stressor that can
strongly influence fertility of herds [25] and also influence
meat quality. Christensen and colleagues demonstrated how
milk toughness could be related to the different exposure of
animals to non comfortable temperatures [26]. Both stressors
produce a negative effect on dairy production and a consid-
erable economic loss.
2.2. Impact of Stress and Environmental Adverse Condi-
tions on Susceptibility to Diseases
Stress conditions have been reported to suppress the im-
mune system and may lead to an increased occurrence of
disease in the presence of pathogens. The immune response
is one of the mechanisms by which animals defend against
different stressors or adverse environmental conditions.
Acute and chronic stress tends to affect the immune re-
sponses in different ways. Chronic stress often suppresses
the immune system thus enhancing the susceptibility of an
animal to disease. On the other side, acute stress often has no
158 Current Protein and Peptide Science, 2014, Vol. 15, No. 2 Bassols et al.
effect on immunity or even sometimes the immune system is
enhanced by stress [27]. Stressors activate the hypothalamic-
pituitary-adrenocortical (HPA) axis and the sympatho-
adrenal medullary axis. Adrenocorticotropic hormone
(ACTH) is the major hormone which regulates the synthesis
and secretion of adrenal glucocorticoids. In turn, the secre-
tion of ACTH in farm animals particularly cows, sheep and
pigs is regulated by corticotrophin-releasing hormone (CRH)
and vasopressin [28]. Additionally, some cytokines like in-
terleukins and tumor necrosis factor have been found to be
involved in pituitary ACTH secretion [29]. The most impor-
tant mediators of the stress response are catecholamines,
epinephrine and norepinephrine, which are the fast-acting
hormones released by the sympathetic nervous system, and
the slow-acting glucocorticoids cortisol and corticosterone,
which are secreted by the adrenal gland after activation of
the HPA axis [18]. The secretion of glucocorticoids and
catecholamines in response to stress has a negative impact on
functions of cells of the immune system in cattle and pigs
and causes reduced lymphocyte proliferation, natural killer
cells activity, neutrophil function and impaired interleukin
and antibody production [30, 31]. Furthermore, glucocorti-
coids upregulate the production of the anti-inflammatory
cytokines IL-4 and IL-10 [32]. Also, the exposure of farm
animals to different stressors, such as long distance transport
and changes in nutrition is associated with an increase in
serum acute phase protein concentrations [33-35]. All those
changes make farm animals susceptible to pathogens with
higher incidence of diseases. Particularly, stress of parturi-
tion and lactation and also long-distance transportation in
dairy cows is associated with increased susceptibility to in-
fectious disease such as mastitis, paratuberculosis, salmonel-
losis and bovine respiratory disease complex and other pro-
duction diseases including infertility, uterine diseases (metri-
tis, retained placenta, prolapsed uterus), ketosis and milk
fever especially during periparturient period [36, 37].
Chronic stress in small ruminants, particularly sheep and
goats, may result in poor welfare and impaired growth, milk
production and reproduction and contribute to the develop-
ment of diseases such as parasitism and enterotoxaemia [38,
39]. In pigs, stress of housing conditions and transportation
could make pigs more susceptible to infectious diseases of
gastrointestinal tract such as post-weaning colibacillosis,
salmonellosis, swine dysentery and porcine proliferative
enteropathies [40]. Also, modern pork production worldwide
cope with porcine respiratory disease complex caused by
multiple viral and bacterial pathogens including porcine re-
productive and respiratory syndrome virus, swine influenza
virus, porcine respiratory coronavirus, Mycoplasma hy-
opneumoniae, Bordetella bronchiseptica, Pasteurella multo-
cida, Actinobacillus pleuropneumoniae and others [41]. A
number of stressors in pigs like marketing, vaccination, cas-
tration, oestrus, parturition and climate conditions can trigger
porcine stress syndrome, which is an inherited neuromuscu-
lar disorder characterized by an abnormal accumulation of
lactic acid in the muscle cells, with a high impact on mortal-
ity as well as on meat quality and composition [42]. In addi-
tion to suppression of the immune system, stress may also
contribute to infections or inflammatory disorders of the gas-
trointestinal system by physiological alterations in the gas-
trointestinal tract. The enteric nervous system normally se-
cretes norepinephrine, the major neurotransmitter in the gas-
trointestinal tract into the mucosa where a variety of bacteria
are presented including food-borne pathogens [43]. Signifi-
cant increases in stress mediators, particularly glucocorti-
coids and catecholamines (epinephrine and norepinephrine),
can affect the status of resident microbiota and disrupt the
intestinal barrier function and increase mucosal permeability
with a consequence of an increased microbial translocation
rate in the gastrointestinal tract. Additionally, stress-related
hormones can alter interactions between the mucosa and
luminal bacteria affecting the commensal microbiota and
leading to an increased passage of pathogenic bacteria [44].
It has been demonstrated that exposure to norepinephrine in
vitro result in a significant increase in Gram-negative bacte-
rial growth. In addition, stress-released norepinephrine in
vitro enhances the virulence of enteropathogens such as
Campylobacter and E. coli (reviewed in [45]). Consequently,
stressed animals are more susceptible to bacterial infections
and a number of farm animals (pigs, cattle and poultry) bring
foodborne pathogens into the abattoirs. Moreover, the expo-
sure to various stressors can increase fecal shedding of en-
teric pathogens, such as E. coli, Salmonella and Campy-
lobacter, leading to an increased cross-contamination during
transport and to a higher degree of carcass contamination
that is the major cause of foodborne disease with a high im-
pact on human health [46]. These aspects will be analyzed in
details in the chapter dedicated to foodborne pathogens.
2.3. Stress-related Oxidative Damage
Many stress conditions have been associated with oxida-
tive stress like weaning, transport [47, 48], and diet [14, 15].
Chronic exposure to stress results in metabolic changes with
damaging effects, in which production of reactive oxygen
species (ROS) and oxidative stress play a major role. Stress
hormones, norepinephrine and glucocorticoids, may contrib-
ute to enhanced formation of reactive oxygen species and
oxidative stress [49, 50]. Oxidative stress is recognized as a
process implicated in many pathophysiological conditions of
farm animals. Aerobic respiration and metabolism generate
reactive oxygen species (ROS) as their by-products arising
mostly from mitochondrial electron transport chain [51].
Cytochrome P-450 enzymes are an important source of ROS
metabolizing either exogenous (xenobiotic) or endogenous
(physiological) substances [52]. ROS comprise two catego-
ries of molecule species: free oxygen radicals and non-
radical ROS. Free oxygen radicals are chemical species con-
taining one or two unpaired electrons. Non-radicals do not
contain unpaired electrons but they are very unstable and can
react with free radicals resulting in a new radical formation
leading to chain reaction of free radical generation. Common
free oxygen radicals include hydroxyl radical (OH), super-
oxide anion (O
2
-
) and nitric oxide (NO) while non-radical
include hydrogen peroxide (H
2
O
2
) [53]. ROS are not always
harmful; they are physiologically used by cells in intracellu-
lar signaling involved in gene expression, cell growth, pro-
tein synthesis, activation of receptors and others. However,
an imbalance between ROS production and their safe re-
moval by antioxidants leads to oxidative stress. Exceeded
amount of ROS can modify cell functions and endanger cell
survival. ROS become stable by acquiring electrons from
lipids, proteins, nucleic acids, and carbohydrates or any other
nearby molecule leading to chain reactions of free radical
molecules formation. Oxidative damages of macromolecules
modify metabolic pathways and change the integrity and
fluidity of cellular membrane resulting in oxidative cell in-
jury, cell death and disease [54]. Among the biological mac-
romolecules being subjects to ROS action, proteins are one
of the most important targets for oxidation and both the pro-
tein expression and their modifications are affected by oxida-
tive stress. Proteins undergo various damages; from protein
cleavage by hydroxyl radical and protein crosslinking to
many side chain modifications. One of the most common
modifications on side chains is carbonyl formation by the
action of very reactive hydroxyl radical or less active oxi-
dants, such as hydroxyl peroxide [55]. These oxidative dam-
ages lead to protein degradation and changes in protein struc-
ture and function modulating important biological processes
within the cells.
Different stressors, external or internal can contribute to
ROS generation. Oxidative stress is considered as a notable
component in the signaling processes involved in inflamma-
tory responses including stimulation of cell adhesion mole-
cules and production of chemo-attractant. During inflamma-
tory conditions, phagocytes produce reactive oxygen species
(ROS) that are needed for killing bacteria [56]. However,
raised amount of ROS can overcome the antioxidant system
and compromise the immune function of farm animals. Low
level of antioxidants can diminish functions of lymphocytes
and macrophages, i.e. their phagocytic ability and microbial
toxicity [57]. In farm animals, oxidative stress is considered
to be involved in pathological conditions relevant to animal
production and general welfare of animals such as mastitis
and reproductive disorders in ruminants, respiratory and en-
teric diseases in cattle and pigs, parasitic diseases in small
ruminants [58, 59]. Some studies have indicated that sup-
plementation of dairy cows with antioxidants, selenium and
vitamin E, enhanced macrophage function and production of
macrophage-derived IL-1, thus improving the immune status
of cows [58, 60]. It has been also suggested that selenium
supplementation in sheep may reduce the susceptibility to
parasitic invasion [61]. Oxidative stress has been found to be
increased in transportation stressed cattle with a higher inci-
dence in respiratory disease [62]; in cows stressed by parturi-
tion and early lactation [63] as well as in cows with mastitis
[59]. Oxidative stress in pigs increases the susceptibility to
diseases, in particular respiratory infections [64]. It has been
also found that even stress due to high density housing con-
dition is related to oxidative damage in pigs [65].
3. PROTEOMICS TOOLS TO EVALUATE STRESS
CONDITIONS AND THEIR IMPACT ON ANIMAL
HEALTH AND WELFARE
The proteome analysis is in general a much greater chal-
lenge than the transcriptome due to the different forms of
proteins in different tissues and biological fluids, including
post-translational modifications. Proteomic techniques have
become an important tool for the study of molecular mecha-
nisms in physiology and etiopathogenesis of diseases. As in
human medicine, a great variety of proteomic approaches
exists also in veterinary sciences, which can be grouped into
two broad categories: gel-based assays and shotgun pro-
teomics. The general advice, also in animal science, is to use
different techniques to better understand the biological ques-
tion, as they are complementary. The best technique for
every sample does not exist.
3.1. Gel-based Approaches
Among the gel based approaches for the separation of
proteins, the two dimensional electrophoresis (2-DE) re-
mains at the moment one of the most used techniques due to
its relative simplicity and an excellent resolving power [66].
In this technique proteins are separated first by isoelectric
point and a further separation is performed by molecular
weight. After the second step, proteins are detected using
visible stains (colloidal Coomassie, silver stain) or fluores-
cent (Sypro, Flamingo, Deep Purple). At this moment several
quantitative limitations remain, due to the sample nature and
low gel to gel reproducibility [67]. In the difference gel elec-
trophoresis (2D-DIGE) the reproducibility problem has been
overcame adding a labelling step prior to 2-DE with three
amino-selective fluorescent dyes with different excitation
wavelenghts (Cy2, Cy3 and Cy5). The use of an internal
standard (Cy2 labelled sample) eliminates gel-to-gel varia-
tion and the parallel separation of different labelled sample
(Cy3-Cy5) into the same gel provides excellent results with a
high statistical power and a lower number of replicates [68].
To investigate quantitative differences between samples,
stained or fluorescent gels have to be digitalized and the im-
ages analyzed with a dedicated software (Progenesis, Decy-
der, Delta 2D). The software workflow integrates sophisti-
cated statistical tools to perform uni- and multi-variate
analysis to simplify complex data elaboration. Identification
of protein spot usually is done by tryptic digestion of pro-
teins and peptide analysis by PMF (peptide mass fingerprint-
ing) using MALDI-TOF (matrix assisted laser desorption
ionization- time of flight) mass spectrometry (MS). Using
PMF protein identification is based only on the mass match-
ing of peptide. To obtain a unique structural information
about the peptides analyzed it is necessary to fragment ion-
ized peptides into the mass spectrometer in MS/MS mode to
achieve the full sequence and to infer with high confidence
the corresponding protein.
3.2. Gel-free Approaches
During recent years gel-free approaches have become
very popular due to the advent of more complete databases
and accurate spectrometers with the advantage also of the
high throughput analysis. The quantitative analysis of pro-
teomes by MS is a crucial point of gel-free approaches and
currently two different methods are used, label-free and la-
bel-based [69]. In the first one unlabeled proteins from a
sample are digested into peptides and separated prior to iden-
tification by MS. The acrylamide gel as a separating system
has been replaced by a liquid chromatography (LC) step at
high or ultra- high pressure (HPLC or UHPLC) with normal
or nano volumes. The most frequently used LC-method
nowadays is the reverse phase chromatography where pep-
tides are separated according to their hydrophobicity on non-
polar columns (C18). To augment resolution it is possible to
couple a second dimension of separation (2D-LC) usually
using a polar column (ion-exchange) that separate peptides
according to charge. After the acquisition of peptide spectral
signals on different mass analyzers (TOF, Orbitrap, FTMS)
the relative amount of all proteins in two or more samples of
interest is calculated using the corresponding peptide inten-
sity between the LC-MS runs [70]. On the other hand the
label-based approach use different pairs (heavy and light) of
isotopic mass-tags covalently linked to the proteins that can
be easily detected by mass spectrometry. Depending on the
type of labelling this strategy can be divided into two more
classes: metabolic labelling and chemical labelling [71]. The
metabolic labelling is an in-vivo labelling technique where
cells or organisms are labelled with different isotopic mole-
cules (salts and/or amino acids) during growth.
14
N/
15
N la-
belling refers to the use of inorganic ions to label cells and
the MS quantitation is done between the ratio of labelled
(
15
N, heavy) and unlabelled (
14
N, light) peptides obtained,
for example, from different experimental classes (con-
trol/diseased). In SILAC labelling (stable isotopic labelling
with amino acids in cell culture) a pair of isotopic aminoac-
ids, usually light and heavy lysine or arginine, are used to
label the cells. In the chemical labelling strategy proteins or
peptides are isotopically or isobarically tagged using a
chemical reaction [72]. Due to the multitude of chemical
features (label and reaction site) that can be used for the la-
belling, several strategies have been developed. Among the
overall amount of approaches iTRAQ and ICAT are the most
used. In the iTRAQ (Isobaric Tags for Relative and Absolute
Quantification) approach is possible to compare up to eight
samples in the same experiment. The tags used are isobaric
and the quantification is done using reporter ions intensities
obtained in the low mass range (m/z 114-121) after the
fragmentation of the differentially labelled peptides in
MS/MS mode [73]. The ICAT (Isotope-Coded Affinity
Tags) approach combines a selective cysteine-reactive group
with light and heavy isotopic tags (8-Da shift) and a biotin-
tag. The latter one is used to purify labelled peptides before
the MS quantitation based on ion intensities of isotopic tags
[70].
3.3. Role of Serum Proteomics in Animal Health Studies
Several proteomic studies highlighted useful results for
diagnosis, pathogenesis, prevention and treatment of com-
mon veterinary diseases. This type of results will be de-
scribed in the following section.
3.3.1. Pigs
From an economical point of view, the most harmful dis-
eases in pig production are PRRS (porcine respiratory and
reproductive syndrome) and PMWS (post-weaning multisys-
temic wasting syndrome).
The etiological agent of PRRS is the PRRS virus
(PRRSV), a virus that belongs to the genus Arterivirus in the
family Arteriviridae and the order Nidovirales. PRRS is
clinically characterized by reproductive losses in late gesta-
tional sows, increased number of weak or stillborn pigs, se-
vere pneumonia in neonatal and nursery pigs, reduction in
growth performances and increased mortality at all ages. The
innate immune response against PRRSV is relatively weak
since one of the defence mechanisms of the virus is to ac-
tively suppress the immune responses and the production of
several key immune-regulatory cytokines [74-76]. Several
proteomics studies have provided information about changes
induced by the virus infection in macrophages, which are the
cells where the virus preferentially infects and replicates [77]
or lungs [78]. In macrophages two proteins involved in stress
response, heat shock 27 kDa protein (HSP27) and superoxide
dismutase 2 (SOD2) were up-regulated [77]. Post-weaning,
multi-systemic wasting syndrome (PMWS) is presently a
major disease problem with significant welfare and eco-
nomic consequences for pig producers. The disease is char-
acterized by wasting, respiratory, enteric and lymphoid sys-
tem problems in young pigs of 4-16 weeks of age [79].
PMWS is considered to be caused by infection by the PCV2
virus, although other factors could be associated to the trig-
gering of the disease. Proteomic studies have shown that
infection of macrophages by the virus causes changes in pro-
teins related to stress response revealing the implication of
oxidative stress in the pathology [80].
Other viral diseases of high interest in porcine production
are Classical swine fever (CSF) and African swine fever
(ASF). CSFV belongs to the genus Pestivirus within the
family Flaviviridae. Virulent strains of classical swine fever
virus (CSFV) provoke severe disease in pigs characterized
by immunosuppression, thrombocytopenia and disseminated
intravascular coagulation, which causes significant economic
losses to the pig industry worldwide [81, 82]. The proteomic
analysis by 2D-DIGE of serum from experimentally infected
pigs at a stage with almost no clinical signs revealed differ-
ential expression of up-regulated and down-regulated pro-
teins in CSFV-infected pigs, involved in blood coagulation,
anti-inflammatory activity and angiogenesis. These proteins
with altered expression may have important implications in
the pathogenesis of classical swine fever [82]. Proteomic
technology was also used to globally examine ASFV-
infected cultured Vero cells in order to determine target pro-
teins for the virus. After 2-DE, the most significant changes
were in redox-related proteins, heat shock proteins and apol-
ipoproteins. These cellular protein modifications could rep-
resent distinct roles during infection related to apoptosis and
transcriptional modulation mechanisms [81]. In both cases,
they may provide a clue for identification of biomarkers for
classical and African swine fever early diagnosis. Foot and
mouth disease (FMD) is another important disease in farm
animal production. Proteomics have been used to analyze
serum protein differences between normal and FMD virus-
infected piglets by LC-MS/MS. Comparing the serum pro-
tein composition before and after FMDV infection, several
proteins were found to be expressed after FMDV infection in
the same piglet (apolipoprotein A-IV precursor, haptoglobin
and probable chemoreceptor glutamine deamidase cheD)
[76]. Authors proposed that these results may provide further
information about biomarkers for early diagnosis of FMD in
piglets. The immune response against a pathogen could be
also explored in the search of immunoreactive proteins,
which could be potential candidates for vaccine production.
This strategy consists usually in the separation of the pro-
teins from a pathogen extract by a 2-DE followed by a west-
ern blot with the serum of diseased or challenged animals
[83]. This technology has been used to identify immunoreac-
tive proteins against Haemophilus parasuis (Glssers dis-
ease) that are considered novel immunogens and candidates
in future vaccines [84]. This approach has also been used to
identify proteins differentially expressed by pathogenic and
non-pathogenic strains of Streptococcus suis. S. suis is an
important swine pathogen with worldwide distribution that is
also responsible for a variety of human diseases. Two studies
have reported the identification of several proteins expressed
only by pathogenic strains and thus they may be considered
putative virulence-associated factors [85, 86]. Diarrhea is a
major challenge in industrial production of pigs, particularly
in neonatal and weaning piglets, being Salmonella typhi-
murium a major cause. The immune reaction of the pig
against the pathogen has been studied in mesenteric lymph
nodes (MLN) of pigs after S. typhimurium infection by
DIGE-based proteomics. The proteome response of porcine
MLN to infection was associated to the induction of proc-
esses such as phagocyte infiltration, cytoskeleton remodeling
and antigen presentation. These results may help to under-
stand the host innate and adaptive immune response of the
animal to control S. typhimurium dissemination in swine
infections [87].
To prevent diarrhea with nutritional supplementation is a
usual procedure in porcine farms. Zinc oxide (ZnO) is an
important dietary factor that regulates intestinal amino acid
and protein metabolism in animals and, given as a supple-
ment to the diet, ameliorates weaning-associated intestinal
injury and growth retardation. Proteomics (2-DE and MS)
helped to understand the underlying mechanisms since it was
shown that zinc supplementation affects the expression of
proteins related to glutathione metabolism and oxidative
stress in the gut. Consistent with the changes in protein ex-
pression, the ratio of reduced glutathione to oxidized glu-
tathione was increased, whereas glutathione-S-transferase
and glutathione peroxidase activities were reduced in ZnO-
supplemented piglets, indicating that ZnO supplementation
improves the redox state and prevents apoptosis in the jeju-
num of weaning piglets, thereby alleviating weaning-
associated diarrhea [88]. In neonatal mammals, the lack of
colostrum is also a frequent cause of diarrhea, since the up-
take of intact immunoglobulins (IgG) from colostrum is
critical for the acquisition of passive immunity and the pre-
vention of intestinal and systemic diseases. The mechanisms
of uptake, the isoforms of IgG taken up by the healthy tissue
and the failure of inflamed gut tissues from pre-term piglets
were also investigated by 2-DE and MS [89].
3.3.2. Cattle
In cattle, one of the major health problems is represented
by mastitis, which is an infection caused by a variety of
pathogens invading the lactating mammary gland, whereas
brucellosis, tuberculosis and viral diseases are most relevant
for their effects on meat production [6]. Several proteomics
studies on serum have been performed in order to detect pu-
tative biomarkers useful for the subclincal diagnoses of mas-
titis [59, 90]. Mastitis is caused by a variety of pathogens
invading the mammary gland. The annual cost associated
with treatment, culling and death of cows as well as loss in
milk production due to mastitis is estimated to be 168 mil-
lion in the UK alone [91]. Furthermore, mastitis severely
compromises the welfare of cows. Early diagnosis and iden-
tification of the causal pathogen are crucial for initiating a
successful antibiotic treatment, ensuring fast recovery and
thereby minimizing the impact on animal health [6]. The
serum proteome of cows affected by subclinical and clinical
mastitis has been addressed above, and a systemic inflamma-
tory and oxidative stress response has been observed in af-
fected animals, being acute phase proteins an important
component of the early phases of the disease [59, 90]. Bru-
cella is a Gram-negative, facultative intracellular bacterium
that is the etiologic agent of bovine brucellosis and causes
chronic infection in humans. In livestock the disease is char-
acterized by abortion and sterility. Proteomics helped to
characterize the immunome of Brucella strains to explain
host specificity and virulence differences among Brucella
species. Thus, the host response to infections with virulent or
attenuated Brucella strains has been analyzed in macro-
phages and other cell types and many virulence factors have
been identified [92]. Proteomic techniques, generally based
in two-dimensional electrophoresis, have enabled the charac-
terization of proteins that could be used as tools to develop
sensitive and specific immunoassays for serodiagnosis of
bovine brucellosis [93], and to identify candidate proteins for
developing better vaccines against Brucella infection in bo-
vine and humans [94]. Johne's disease (JD) is a widespread
and economically important chronic inflammatory disease of
the small intestine of ruminants caused by Mycobacterium
avium subsp. paratuberculosis (MAP), characterized by se-
vere emaciation that poses a significant economic problem to
the beef and dairy industry worldwide. Although there are
several techniques available for diagnosis of JD, their sensi-
tivity is questionable. A combination of several techniques
(2D-DIGE, LC-MS/MS, iTRAQ) has been useful for novel
biomarkers of MAP infection [95], to characterize the differ-
ential proteome of Type I and Type II MAP, which are dis-
tinct and appear to have different host preferences [96], and
to provide further information about the pathogenesis of the
disease [97]. An immunoproteomic approach has also helped
to identify candidate proteins for use antigens for improved
serodiagnostic tests for bovine paratuberculosis [98, 99]. The
background infection with MAP is high and it may confound
the detection of bovine tuberculosis caused by similar myco-
bacteria (M. bovis). In this case, a proteomic approach has
been used to detect differentially expressed proteins in the
serum of animals infected by one or the other pathogen, con-
tributing to the development of mycobacterium specific tools
[100]. Viral diseases are also important pathologies in cattle.
Bovine viral diarrhea virus (BVDV) infection is widespread
in cattle worldwide, causing important economic losses.
Pathogenesis of the disease caused by BVDV is complex,
due to the existence of several strains and biotypes. BVDV
can cause a persistent latent infection and immune suppres-
sion if animals are infected during early gestation. The mo-
lecular mechanisms that underscore the complex disease
etiology leading to immune suppression in cattle caused by
BVDV have been addressed by evaluating the effect of
BVDV infection of bovine monocytes to determine their role
in viral immune suppression and uncontrolled inflammation
[101, 102]. Other cattle diseases that have been studied by
using proteomics are claw horn disruption (CHD), a common
underlying cause of lameness in dairy cattle which leads to
compromised animal welfare and production losses, with the
characterization of three different claw tissues [103] and
milk fever, an important metabolic disorder of dairy cows
after calving, characterized by hypocalcemia, tetany, lateral
recumbency, and eventual coma [104].
3.4. Role of Serum Proteomics in Animal Welfare Studies
Proteomics has been used to identify new potential stress
biomarkers in pigs housed at different densities since insuffi-
cient space allowances induce a repeated state of stress that
alters the activity of the pituitaryadrenal axis, behavior and
reproduction [105, 106]. Elsewhere, it was shown that the
use of 2D-DIGE allowed the identification of actin as a po-
tential biomarker of stress [65]. 2D-DIGE was also used to
analyze the serum proteome of cows maintained under dif-
ferent management systems (good and semiferal conditions),
showing an involvement of the redox system as the main
adaptation of cows living in challenging environmental con-
ditions [107].
Likewise, the stresses of transportation, weaning and
commingling are associated with an increased incidence of
bacterial and viral pneumonia in cattle. The interaction be-
tween both conditions has been examined by 2-DE in the
epithelial lining fluid of bovine respiratory tract, showing
that stress causes protein changes in pulmonary fluids, sug-
gesting a mechanism through which stress alters respiratory
disease susceptibility [108]. Similarly, the proteomes of bo-
vine serum samples have been characterized and used to-
gether with other OMICS to discriminate between the bio-
logical responses to stress or infection (bovine respiratory
disease (BRD)), showing that the changes produced in the
serum profile are different depending on the causing effect
[62].
Nutrition is an important component of welfare. In dairy
cows, ketosis is a common metabolic disorder that is fre-
quently observed during the early lactation period. Evalua-
tion of oxidative stress has increasingly contributed to the
understanding of the fundamental mechanisms involved in
metabolic disorders [57, 63]. The molecular pathways acti-
vated in the liver of the ketotic cow were also studied by 2-
DE coupled to MALDI-MS/MS to compare the liver pro-
teomic profile between ketotic and normal cows. The differ-
entially expressed proteins play a role in energy metabolism,
carbohydrate degradation, fatty acid metabolism, amino acid
metabolism, antioxidation, cell structure, nucleotide metabo-
lism, and protein metabolism [109]. Ketosis is due to a nega-
tive energy balance of the individual, and appears when the
energy demand for maintenance and lactation exceeds that of
dietary energy intake, very frequently around calving. The
hypothalamus is the central regulatory unit that balances a
number of body functions including metabolic rate, hunger,
and satiety signals, and respond to alterations of circulating
nutrients and hormones that reflect the peripheral energy
status. To understand such a control, the hypothalami from
fed and energy restricted cows were characterized using pro-
teomic techniques, leading to the identification of several
proteins involved in energy and nucleotide metabolism, and
oxidative stress under conditions of dietary energy defi-
ciency [110, 111]. Other researchers have focused their at-
tention on the effects of body weight and nutrition on mam-
mary parenchymal tissue protein expression profiles in heif-
ers mammary development by using a proteomic approach
[112].
In pigs, the relation between the type of diet and the oxi-
dative status of the individual has been also studied by pro-
teomics. Thus, a diet based on a soy protein diet (SPI) sig-
nificantly changes the hepatic transcription pattern compared
with a casein diet showing an increased oxidative stress re-
sponse and significant effects on protein biosynthesis [113].
The possibility that maternal diets during gestation could
affect growth and tissue development of offspring and pro-
gram their later phenotype is an emerging challenge in pig
production. This issue has been addressed by investigating
the effects of protein levels in diets of pregnant sows on the
proteomic features of subcutaneous adipose tissue (SCAT) of
the offspring at birth and its possible persistence later in age
(6 months old). Modifications in SCAT protein abundance
shortly after birth were investigated by 2-DE and MS. In this
study, a higher abundance of proteins involved in pathways
related to glucose and fatty acid metabolisms, lipid transport,
and regulation of apoptosis were found in low protein-piglets
in comparison with control piglets [114]. Finally, the mo-
lecular expression changes that occur during pregnancy were
analyzed in porcine peripheral blood mononuclear cells
(PBMC) using proteomic analysis. By classifying the pro-
teins according to their functions, a large number of differen-
tially regulated proteins involved in anti-oxidant, detoxifica-
tion and stress response pathways were found, upregulated
during pregnancy [115].
3.5. Proteomics of Other Body Fluids in Farm Animals
Serum and plasma are the most frequently used biologi-
cal samples for monitoring health and disease in farm ani-
mals. Blood is an easy sample to obtain, but increasing atten-
tion is being paid Animal welfare to other, noninvasive sam-
ples, such as milk and saliva, since their compositions may
reflect the overall health status of the individual animal [116-
118].
3.6. Milk
Comparative proteomic analyses of bovine milk have
emerged in recent years [8]. Milk and whey have been thor-
oughly studied in mastitic cows. Normal and mastitis whey
showed a very different composition, likely due to extravasa-
tion of blood proteins to the mammary gland [119]. Different
isoforms from the most abundant protein in milk, casein,
were detected in both normal and mastitis whey. Other pro-
teins, such as lactotransferrin, serotransferrin and many cel-
lular proteins were only detected in the inflamed animal
samples. They are responsible for the great change in com-
position between normal and mastitis whey, especially those
which exert a biological function related to immune defense
[90, 120]. The differential response to infection by Gram-
negative and Gram-positive bacteria has been analyzed in
whey from cows naturally infected with E. coli or S. aureus
[121, 122]. S. aureus is one of the most prevalent pathogens
to cause mastitis in dairy cattle. Intramammary infection of
dairy cows with S. aureus is often subclinical but can lead to
chronic infection, due to the pathogen's ability to evade the
innate defense mechanisms. Proteomic analysis of the milk
following intramammary infection revealed unique host pro-
tein expression profiles that were dependent on the infecting
strain as well as the phase of infection, and allowed the iden-
tification of potential antimicrobial peptide involved in host
defense [123]. Intramammary infusion of lipopolysaccharide
(LPS) that simulates mastitis caused by Gram-negative bac-
teria and mammary epithelial cells stimulated with heat inac-
tivated E. coli o S. aureus strains have been also used as ex-
perimental approaches for the study of the pathogenesis and
biological response in mastitis [59, 121, 124].
3.7. Saliva
The benefit of saliva as a specimen is that sample collec-
tion is not invasive, hence allowing frequent sampling. Sa-
liva is an extraordinary fluid in terms of research and diag-
nostic possibilities. Its composition in electrolytes, hormones
and especially its proteome contains information about feed-
ing status, nutritional requirements and adaptations to diet
and environment, and also about health status of animals.
Therefore, the analysis of salivary proteomes is emerging as
a tool to identify animal disease biomarkers and to better
understand animal physiology [116-118, 125].
4. FOODBORNE PATHOGENS AND PROTEOMICS
Food safety encloses different aspects, from genetically
modified organisms (GMO), to illegal treatment of animals
up to foodborne pathogens that can produce toxins danger-
ous to humans. Proteomics applied to the study of food can
help to counteract such public health problems, in particular
those related to the presence and growth of foodborne patho-
gens. Fig. 3 resumes the current applications of proteomics
in the field of microbial food safety; most of literature de-
scribes the immunoproteomic approach to detect specific
immunoreactive epitopes that can be detected through the
application of a targeted (SRM- MS MS) analysis of proteo-
typic peptides of bacteria of interest.
4.1. Salmonella spp.
Salmonella spp. colonise all the major livestock species
and very often food-producing animals, which may be as-
ymptomatic. This represents a problem because of the possi-
ble production of contaminated meat and other food prod-
ucts. Furthermore, Salmonella is an adaptable microorgan-
ism that could be present in fresh products and also survive
in presence of preservatives and additives. Calhoun and col-
leages [2] described, using a comparative proteomic ap-
proach, the effect of propionic acid (PA), a common food
preservative agent, on the metabolism of Salmonella. This
work provides a comprehensive analysis of differentially
expressed proteins between the unadapted and PA adapted
condition. Furthermore, the study of variation of protein ex-
pression on PA adapted cells, gave new insights to describe
new putative virulence factors of this organism.
Another interesting paper of Kim and colleagues [126]
describes the setup of a quantitative method to detect Salmo-
nella spp. with a modified SILAC procedure. Authors identi-
fied and reported 76 proteins from a strain of Salmonella
enterica serovar Enteritidis, which were differentially ex-
pressed during exposition to H
2
O
2
oxidative stress. The final
result is a protein, SP1, that could be very interesting as
marker of systemic infection in an animal host.
4.2. Campylobacter spp.
On the basis of data available from European Union
(EFSA), Campylobacter spp. is considered the major cause
of acute food poisoning mediated by bacteria [127]. Fur-
thermore, the incidence of this foodborne pathogen varies
between years and countries for unknown reasons. Poultry is
the major reservoir of this pathogen, and C. jejeuni, the more
representative of this class, cannot grow outside a host. Fur-
thermore, Campylobacter has a strong capacity to colonise
new niches because of its formidable mechanisms of adapta-
tion to different environmental stressors, including antibiot-
ics. Due to the unclear mechanism of infection, the majority
of literature about Campylobacter is focused on the elucida-
tion of infection mechanisms, as reported, for example, by
Elmi and colleagues. [128]. These authors used proteomic
techniques to identify outer membrane vesicles proteins

Fig. (3). General strategies of proteomics approaches useful for foodborne pathogen investigation.
(OMV) and investigated the mechanisms of interaction be-
tween Campylobacter OMV and intestinal epithelial cells,
with particular attention to the induction of the host innate
immune response. Authors discovered the presence of N-
linked glycoproteins associated with OMV participating in
this mechanism. Liu and colleagues [129] performed a pro-
teomic analysis of proteins extracted from different C. jeje-
uni isolates by LC-MS/MS and demonstrated a remodelling
of the C. jejuni proteome that occurs within cultured mam-
malian cells, attributable to specific adaptation to the intra-
cellular environment. This fact may explain the difficulties to
growth this pathogen under standard laboratory conditions.
4.3. Listeria
Listeria monocytogenes is an opportunistic foodborne
pathogen that can cause listeriosis. It has been estimated that
in the United States alone is responsible for 28% of all food-
related deaths [130]. The most susceptible targets are im-
munocompromised patients, neonates and pregnant women.
The more frequent reservoirs of L. monocytogenes appear to
be soil and mammalian GI tracts that contaminate vegetation.
Grazing animals can ingest the microorganism and further
contaminate vegetation and soil. This is a disease character-
ized by oral-fecal transmission. One of the most dangerous
features of these bacteria is its adaptative capacity. A pro-
teomic study demonstrated how this microorganism is ex-
tremely versatile in its adaptive mechanisms to cold. The
study highlighted that protein synthesis and folding, nutrient
uptake and oxidative stress pathways were the most impor-
tant pathways involved in cold adaptation response. The
gained knowledge is important to evaluate the possibility of
an intervention to counteract its growth at cold temperatures
[131]. Moreover, the differential protein expression of L.
monocytogenes pathogen growing under the presence of high
concentrations of bile salts has been described, showing dif-
ferences in the expression of proteins involved in biofilm
formation, transmembrane efflux pumps and osmotic stress
response. This data demonstrates how variability among
strains could be a key component of Listeria virulence [132].
4.4. E. coli
At least six groups of E. coli have been isolated from the
gut of mammalian hosts (humans and other animals); among
them Vero cytotoxin producing E. coli (VTEC strains) and
E. coli O157:H7, which are widely recognized as important
cause of foodborne disease in the last two decades. Cattle are
the most important reservoirs of E. coli O157:H7 that is the
major cause of outbreaks in humans. It has documented how
most outbreaks are indeed due to improper food handling
practices and to the consumption of undercooked meat [133,
134]. These strains of E. coli are normally present in the gut
of asymptomatic cattle but they can often contaminate beef
meat, minced and other derived products for human con-
sumption, including milk [134].
As other foodborne pathogens, E. coli has the ability to
continuously evolve into new types that are never character-
ized. From this point of view, proteomics is an important
tool to understand the mechanisms of evolution of this
pathogen. The proteome of E. coli has already been well
characterized [135]. An important problem related to this
infection is antibiotic resistance, a phenomenon that has been
associated to the treatment of animals with sub therapeutic
doses of antibiotics as a preventive measure in farms. Pro-
teomics, in particular 2D-DIGE coupled with MS, have been
used to study the effect of triclosan, a disinfectant used for
several strains of wild type and E. coli O157:H19. Interest-
ingly, authors described that triclosan tolerance acts trough
several concerted mechanisms to achieve high-level resis-
tance, involving quorum sensing pathways [136].
Another interesting work that attempts the elucidation of
the of antibiotic multiresistance mechanism, a big issue in
animal breeding, has been reported by Piras and colleagues
[137], who used a proteomic approach based on 2-DE cou-
pled with MS/MS to reveal that antibiotic multiresistance
(more than 4 antibiotics) in E. coli from buffalo species in-
volves proteins of quorum sensing, such as autoinducer II
and Lux S.
CONCLUDING REMARKS
It is clear that numerous aspects can contribute to shape
the entire chain from farm to fork. About this topic animal
stress and animal welfare are strictly linked to the subsequent
food safety and quality. Proteomics represents a relatively
new way of thinking that, thanks to the dramatic increase
of innovative techniques, is able to help in the discovery of
new ways to improve general management of animals, wel-
fare, monitoring immunoresponse and faster diagnosis of
disease with particular attention to subclinical diseases. Last,
but not the least, microbial proteomics is a valid method to
revolutionize the classic approach to diagnosis. Through
proteomics it is possible to understand the mechanism of
infection and consequently to counteract it, earn money and
avoid the use of antibiotics (and mutiresistance). Proteomics
should be considered a valid help for public health, and can
be adopted to upgrade and improve some protocols that
could be used in official surveillance and test development.
CONFLICT OF INTEREST
The authors confirm that this article content has no con-
flicts of interest.
ACKNOWLEDGEMENTS
The authors are grateful to COST ACTION FA1002-
Farm Animal Proteomics- for network provided.
REFERENCES
[1] Lykkesfeldt, J.; Svendsen, O. Oxidants and antioxidants in disease:
oxidative stress in farm animals. Vet. J., 2007, 173(3), 502-511.
[2] Calhoun, L.N.; Liyanage, R.; Lay, J.O., Jr.; Kwon, Y.M. Proteomic
analysis of Salmonella enterica serovar Enteritidis following
propionate adaptation. BMC Microbiol., 2010, 10, 249.
[3] Caperna, T.J.; Shannon, A.E.; Blomberg Le, A.; Garrett, W.M.;
Ramsay, T.G. Identification of protein carbonyls in serum of the
fetal and neonatal pig. Comp. Biochem. Physiol. B. Biochem. Mol.
Biol., 2010, 156(3), 189-196.
[4] Roncada, P.; Begni, B.; Amadori, M.; Cristoni, S.; Archetti, I.L.;
Boldetti, C.; Fortin, R.; Deriu, F.; Greppi, G.F. Blood serum
proteome for welfare evaluation in pigs. Vet. Res. Commun., 2007,
31 Suppl 1, 321-325.
[5] Bonizzi, L.; Roncada, P. Welfare and immune response. Vet. Res.
Commun., 2007, 31 Suppl 1, 97-102.
[6] Bendixen, E.; Danielsen, M.; Hollung, K.; Gianazza, E.; Miller, I.
Farm animal proteomics--a review. J. Proteomics, 2011, 74(3),
282-293.
[7] Marcelino, I.; de Almeida, A.M.; Ventosa, M.; Pruneau, L.; Meyer,
D.F.; Martinez, D.; Lefranois, T.; Vachiry, N.; Coelho, A.V.
Tick-borne diseases in cattle: Applications of proteomics to
develop new generation vaccines. J. Proteomics, 2012, 75(14),
4232-4250.
[8] Roncada, P.; Piras, C.; Soggiu, A.; Turk, R.; Urbani, A.; Bonizzi,
L. Farm animal milk proteomics. J Proteomics, 2012, 75(14),
4259-4274.
[9] Veissier, I.; Boissy, A. Stress and welfare: two complementary
concepts that are intrinsically related to the animal's point of view.
Physiology & Behavior, 2007, 92(3), 429-433.
[10] Blokhuis, H.J.; Hopster, H.; Geverink, N.A.; Korte, S.M.; Reenen,
C.G. Studies of stress in farm animals. Comparative Haematology
International, 1998, 8(2), 94-101.
[11] Dhabhar, F.S.; McEwen, B.S. Acute stress enhances while chronic
stress suppresses cell-mediated immunity in vivo: a potential role
for leukocyte trafficking. Brain Behav. Immun., 1997, 11(4), 286-
306.
[12] Moberg, G.P.; Mench, J.A. The biology of animal stress : basic
principles and implications for animal welfare. CABI Publishing:
Wallingford, 2000.
[13] Mormede, P.; Andanson, S.; Auperin, B.; Beerda, B.; Guemene,
D.; Malmkvist, J.; Manteca, X.; Manteuffel, G.; Prunet, P.; van
Reenen, C.G.; Richard, S.; Veissier, I. Exploration of the
hypothalamic-pituitary-adrenal function as a tool to evaluate
animal welfare. Physiology & Behavior, 2007, 92(3), 317-339.
[14] Megahed, G.A.; Anwar, M.M.; Wasfy, S.I.; Hammadeh, M.E.
Influence of heat stress on the cortisol and oxidant-antioxidants
balance during oestrous phase in buffalo-cows (Bubalus bubalis):
thermo-protective role of antioxidant treatment. Reprod. Domest.
Anim., 2008, 43(6), 672-677.
[15] Tanaka, M.; Kamiya, Y.; Suzuki, T.; Nakai, Y. Changes in
oxidative status in periparturient dairy cows in hot conditions.
Anim. Sci. J., 2011, 82(2), 320-324.
[16] Lomborg, S.R.; Nielsen, L.R.; Heegaard, P.M.; Jacobsen, S. Acute
phase proteins in cattle after exposure to complex stress. Vet. Res.
Commun., 2008, 32(7), 575-582.
[17] Pineiro, M.; Pineiro, C.; Carpintero, R.; Morales, J.; Campbell,
F.M.; Eckersall, P.D.; Toussaint, M.J.; Lampreave, F.
Characterisation of the pig acute phase protein response to road
transport. Vet. J., 2007, 173(3), 669-674.
[18] Dhabhar, F.S. Enhancing versus suppressive effects of stress on
immune function: implications for immunoprotection and
immunopathology. Neuroimmunomodulation, 2009, 16(5), 300-
317.
[19] Kadzere, C.T.; Murphy, M.R.; Silanikove, N.; Maltz, E. Heat stress
in lactating dairy cows: a review. Livestock Production Science,
2002, 77(1), 59-91.
[20] Lu, C.D. Effects of heat stress on goat production. Small Ruminant
Research, 1989, 2(2), 151-162.
[21] Marai, I.F.M.; El-Darawany, A.A.; Fadiel, A.; Abdel-Hafez,
M.A.M. Physiological traits as affected by heat stress in sheepA
review. Small Ruminant Research, 2007, 71(13), 1-12.
[22] White, H.M.; Richert, B.T.; Schinckel, A.P.; Burgess, J.R.; Donkin,
S.S.; Latour, M.A. Effects of temperature stress on growth
performance and bacon quality in grow-finish pigs housed at two
densities. J. Anim. Sci., 2008, 86(8), 1789-1798.
[23] Carroll, J.A.; Burdick, N.C.; Chase Jr, C.C.; Coleman, S.W.;
Spiers, D.E. Influence of environmental temperature on the
physiological, endocrine, and immune responses in livestock
exposed to a provocative immune challenge. Domestic Animal
Endocrinology, 2012, 43(2), 146-153.
[24] Coubrough, R. Stress and fertility. A review. The Onderstepoort
journal of veterinary research, 1985, 52(3), 153.
[25] De Rensis, F.; Scaramuzzi, R.J. Heat stress and seasonal effects on
reproduction in the dairy cow--a review. Theriogenology, 2003,
60(6), 1139-1151.
[26] Christensen, L.; Ertbjerg, P.; Lje, H.; Risbo, J.; van den Berg,
F.W.; Christensen, M. Relationship between meat toughness and
properties of connective tissue from cows and young bulls heat
treated at low temperatures for prolonged times. Meat science,
2012.
[27] Salak-Johnson, J.L.; McGlone, J.J. Making sense of apparently
conflicting data: Stress and immunity in swine and cattle. J. Anim.
Sci., 2007, 85(13 suppl), E81-E88.
[28] Minton, J.E. Function of the hypothalamic-pituitary-adrenal axis
and the sympathetic nervous system in models of acute stress in
domestic farm animals. J. Anim. Sci., 1994, 72(7), 1891-1898.
[29] Whitnall, M.H. Regulation of the hypothalamic corticotropin-
releasing hormone neurosecretory system. Progress in
Neurobiology, 1993, 40(5), 573-629.
[30] Mallard, B.A.; Dekkers, J.C.; Ireland, M.J.; Leslie, K.E.; Sharif, S.;
Vankampen, C.L.; Wagter, L.; Wilkie, B.N. Alteration in immune
responsiveness during the peripartum period and its ramification on
dairy cow and calf health. J. Dairy Sci., 1998, 81(2), 585-595.
[31] Salak, J.L.; McGlone, J.J.; Lyte, M. Effects of in vitro
adrenocorticotrophic hormone, cortisol and human recombinant
interleukin-2 on porcine neutrophil migration and luminol-
dependent chemiluminescence. Vet. Immunol. Immunopathol.,
1993, 39(4), 327-337.
[32] Webster Marketon, J.I.; Glaser, R. Stress hormones and immune
function. Cell Immuno.l, 2008, 252(1-2), 16-26.
[33] Arthington, J.D.; Eicher, S.D.; Kunkle, W.E.; Martin, F.G. Effect
of transportation and commingling on the acute-phase protein
response, growth, and feed intake of newly weaned beef calves. J.
Anim. Sci., 2003, 81(5), 1120-1125.
[34] Pieiro, C.; Pieiro, M.; Morales, J.; Carpintero, R.; Campbell,
F.M.; Eckersall, P.D.; Toussaint, M.J.M.; Alava, M.A.;
Lampreave , F. Pig acute-phase protein levels after stress induced
by changes in the pattern of food administration. Animal, 2007,
1(01), 133-139.
[35] Saco, Y.; Docampo, M.J.; brega, E.; Manteca, X.; Diestre, A.;
Lampreave, F.; Bassols, A. Effect of transport stress on serum
haptoglobin and pig-MAP in pigs. Animal Welfare, 2003, 12(3),
403-409.
[36] Kimura, K.; Reinhardt, T.A.; Goff, J.P. Parturition and
hypocalcemia blunts calcium signals in immune cells of dairy
cattle. J. Dairy Sci., 2006, 89(7), 2588-2595.
[37] Nir Markusfeld, O. What are production diseases, and how do we
manage them? Acta. Ve.t Scand. Suppl., 2003, 98, 21-32.
[38] Dwyer, C.M.; Bornett, H.L.I. Chronic stress in sheep: assessment
tools and their use in different management conditions. Animal
Welfare, 2004, 13(3), 293-304.
[39] Uzal, F.A. Diagnosis of Clostridium perfringens intestinal
infections in sheep and goats. Anaerobe, 2004, 10(2), 135-143.
[40] Pluske, J.R.; Pethick, D.W.; Hopwood, D.E.; Hampson, D.J.
Nutritional influences on some major enteric bacterial diseases of
pig. Nutrition Research Reviews, 2002, 15(02), 333-371.
[41] Brockmeier, S.L.; Loving, C.L.; Nicholson, T.L.; Palmer, M.V.
Coinfection of pigs with porcine respiratory coronavirus and
Bordetella bronchiseptica. Vet. Microbiol., 2008, 128(1-2), 36-47.
[42] Caine, W.R.; Schaefer, A.L.; Aalhus, J.L.; Dugan, M.E.R.
Behaviour, growth performance and pork quality of pigs differing
in porcine stress syndrome genotype receiving dietary magnesium
aspartate hydrochloride. Canadian Journal of Animal Science,
2000, 80(1), 175-182.
[43] Hart, A.; Kamm, M.A. Mechanisms of initiation and perpetuation
of gut inflammation by stress. Alimentary Pharmacology &
Therapeutics, 2002, 16(12), 2017-2028.
[44] Lyte, M.; Vulchanova, L.; Brown, D. Stress at the intestinal
surface: catecholamines and mucosabacteria interactions. Cell and
Tissue Research, 2011, 343(1), 23-32.
[45] Rostagno, M.H. Can stress in farm animals increase food safety
risk? Foodborne Pathog. Dis., 2009, 6(7), 767-776.
[46] Verbrugghe, E.; Boyen, F.; Gaastra, W.; Bekhuis, L.; Leyman, B.;
Van Parys, A.; Haesebrouck, F.; Pasmans, F. The complex
interplay between stress and bacterial infections in animals. Vet.
Microbiol., 2012, 155(24), 115-127.
[47] Burke, N.C.; Scaglia, G.; Boland, H.T.; Swecker, W.S.; Jr.
Influence of two-stage weaning with subsequent transport on body
weight, plasma lipid peroxidation, plasma selenium, and on
leukocyte glutathione peroxidase and glutathione reductase activity
in beef calves. Vet. Immunol. Immunopathol., 2009, 127(3-4), 365-
370.
[48] Chirase, N.K.; Greene, L.W.; Purdy, C.W.; Loan, R.W.;
Auvermann, B.W.; Parker, D.B.; Walborg, E.F.; Jr.; Stevenson,
D.E.; Xu, Y.; Klaunig, J.E. Effect of transport stress on respiratory
disease, serum antioxidant status, and serum concentrations of lipid
peroxidation biomarkers in beef cattle. Am. J. Vet. Res., 2004,
65(6), 860-864.
[49] Behl, C.; Lezoualc'h, F.; Trapp, T.; Widmann, M.; Skutella, T.;
Holsboer, F. Glucocorticoids enhance oxidative stress-induced cell
death in hippocampal neurons in vitro. Endocrinology, 1997,
138(1), 101-106.
[50] Mao, W.; Iwai, C.; Keng, P.C.; Vulapalli, R.; Liang, C.S.
Norepinephrine-induced oxidative stress causes PC-12 cell
apoptosis by both endoplasmic reticulum stress and mitochondrial
intrinsic pathway: inhibition of phosphatidylinositol 3-kinase
survival pathway. Am. J. Physiol. Cell Physiol., 2006, 290(5),
C1373-1384.
[51] Valko, M.; Leibfritz, D.; Moncol, J.; Cronin, M.T.; Mazur, M.;
Telser, J. Free radicals and antioxidants in normal physiological
functions and human disease. Int. J. Biochem. Cell Biol., 2007,
39(1), 44-84.
[52] Miller, J.K.; Brzezinska-Slebodzinska, E.; Madsen, F.C. Oxidative
stress, antioxidants, and animal function. J Dairy Sci., 1993, 76(9),
2812-2823.
[53] Shackelford, R.E.; Kaufmann, W.K.; Paules, R.S. Oxidative stress
and cell cycle checkpoint function. Free Radic. Biol. Med., 2000,
28(9), 1387-1404.
[54] Nordberg, J.; Arner, E.S. Reactive oxygen species, antioxidants,
and the mammalian thioredoxin system. Free Radic. Biol. Med.,
2001, 31(11), 1287-1312.
[55] Barelli, S.; Canellini, G.; Thadikkaran, L.; Crettaz, D.; Quadroni,
M.; Rossier, J.S.; Tissot, J.D.; Lion, N.; Oxidation of proteins:
Basic principles and perspectives for blood proteomics. Proteomics
Clin. Appl., 2008, 2(2), 142-157.
[56] Thannickal, V.J.; Fanburg, B.L. Reactive oxygen species in cell
signaling. Am. J. Physiol. Lung Cell Mol. Physiol., 2000, 279(6),
L1005-1028.
[57] Sordillo, L.M.; Aitken, S.L. Impact of oxidative stress on the health
and immune function of dairy cattle. Vet. Immunol. Immunopathol,
2009, 128(1-3), 104-109.
[58] Politis, I.; Bizelis, I.; Tsiaras, A.; Baldi, A. Effect of vitamin E
supplementation on neutrophil function, milk composition and
plasmin activity in dairy cows in a commercial herd. J. Dairy Res.,
2004, 71(3), 273-278.
[59] Turk, R.; Piras, C.; Kovacic, M.; Samardzija, M.; Ahmed, H.; De
Canio, M.; Urbani, A.; Mestric, Z.F.; Soggiu, A.; Bonizzi, L.;
Roncada, P. Proteomics of inflammatory and oxidative stress
response in cows with subclinical and clinical mastitis. J.
Proteomics, 2012, 75(14), 4412-4428.
[60] Politis, I.; Hidiroglou, M.; Batra, T.R.; Gilmore, J.A.; Gorewit,
R.C.; Scherf, H. Effects of vitamin E on immune function of dairy
cows. Am. J. Vet. Res., 1995, 56(2), 179-184.
[61] Celi, P.; Eppleston, J.; Armstrong, A.; Watt, B. Selenium
supplementation increases wool growth and reduces faecal egg
counts of Merino weaners in a selenium-deficient area. Animal
Production Science, 2010, 50(7), 688-692.
[62] Aich, P.; Jalal, S.; Czuba, C.; Schatte, G.; Herzog, K.; Olson, D.J.;
Ross, A.R.; Potter, A.A.; Babiuk, L.A.; Griebel, P. Comparative
approaches to the investigation of responses to stress and viral
infection in cattle. OMICS, 2007, 11(4), 413-434.
[63] Turk, R.; Juretic, D.; Geres, D.; Svetina, A.; Turk, N.; Flegar-
Mestric, Z. Influence of oxidative stress and metabolic adaptation
on PON1 activity and MDA level in transition dairy cows. Anim.
Reprod. Sci., 2008, 108(1-2), 98-106.
[64] Deblanc, C.; Robert, F.; Pinard, T.; Gorin, S.; Queguiner, S.;
Gautier-Bouchardon, A.V.; Ferre, S.; Garraud, J.M.; Cariolet, R.;
Brack, M.; Simon, G. Pre-infection of pigs with Mycoplasma
hyopneumoniae induces oxidative stress that influences outcomes
of a subsequent infection with a swine influenza virus of H1N1
subtype. Vet. Microbiol., 2013, 162(2-4), 643-651.
[65] Marco-Ramell, A.; Pato, R.; Pena, R.; Saco, Y.; Manteca, X.; Ruiz
de la Torre, J.L.; Bassols, A. Identification of serum stress
biomarkers in pigs housed at different stocking densities. Vet. J.,
2011, 190(2), e66-71.
[66] Gorg, A.; Weiss, W.; Dunn, M.J. Current two-dimensional
electrophoresis technology for proteomics. Proteomics, 2004,
4(12), 3665-3685.
[67] Rabilloud, T.; Chevallet, M.; Luche, S.; Lelong, C. Two-
dimensional gel electrophoresis in proteomics: Past, present and
future. J. Proteomics, 2010, 73(11), 2064-2077.
[68] Minden, J.S. DIGE: past and future. Methods Mol. Biol., 2012, 854,
3-8.
[69] Soares, R.; Franco, C.; Pires, E.; Ventosa, M.; Palhinhas, R.; Koci,
K.; Martinho de Almeida, A.; Varela Coelho, A. Mass
spectrometry and animal science: protein identification strategies
and particularities of farm animal species. J. Proteomics, 2012,
75(14), 4190-4206.
[70] Shiio, Y.; Aebersold, R. Quantitative proteome analysis using
isotope-coded affinity tags and mass spectrometry. Nat. Protoc.,
2006, 1(1), 139-145.
[71] Bantscheff, M.; Schirle, M.; Sweetman, G.; Rick, J.; Kuster, B.
Quantitative mass spectrometry in proteomics: a critical review.
Anal. Bioanal. Chem., 2007, 389(4), 1017-1031.
[72] Ong, S.E. The expanding field of SILAC. Anal. Bioanal Chem.,
2012, 404(4), 967-976.
[73] Aggarwal, K.; Choe, L.H.; Lee, K.H. Shotgun proteomics using the
iTRAQ isobaric tags. Brief Funct. Genomic Proteomic, 2006, 5(2),
112-120.
[74] Cho, J.G.; Dee, S.A. Porcine reproductive and respiratory
syndrome virus. Theriogenology, 2006, 66(3), 655-662.
[75] Lunney, J.K.; Benfield, D.A.; Rowland, R.R. Porcine reproductive
and respiratory syndrome virus: an update on an emerging and re-
emerging viral disease of swine. Virus Res., 2010, 154(1-2), 1-6.
[76] Liu, J.; Bai, J.; Lu, Q.; Zhang, L.; Jiang, Z.; Michal, J.J.; He, Q.;
Jiang, P. Two-dimensional liquid chromatography-tandem mass
spectrometry coupled with isobaric tags for relative and absolute
quantification (iTRAQ) labeling approach revealed first proteome
profiles of pulmonary alveolar macrophages infected with porcine
circovirus type 2. J. Proteomics, 2013, 79, 72-86.
[77] Zhang, H.; Guo, X.; Ge, X.; Chen, Y.; Sun, Q.; Yang, H. Changes
in the cellular proteins of pulmonary alveolar macrophage infected
with porcine reproductive and respiratory syndrome virus by
proteomics analysis. J. Proteome Res., 2009, 8(6), 3091-3097.
[78] Xiao, S.; Wang, Q.; Jia, J.; Cong, P.; Mo, D.; Yu, X.; Qin, L.; Li,
A.; Niu, Y.; Zhu, K.; Wang, X.; Liu, X.; Chen, Y. Proteome
changes of lungs artificially infected with H-PRRSV and N-
PRRSV by two-dimensional fluorescence difference gel
electrophoresis. Virol J., 2010, 7, 107.
[79] Banks, M.; Grierson, S.; Tucker, D.; Bailey, M.; Donadeau, M.;
Sargent, C.; King, D.; Mellencamp, M. Swine and circovirus. Dev.
Biol (Basel), 2006, 126, 107-113; discussion 325-106.
[80] Ramirez-Boo, M.; Nunez, E.; Jorge, I.; Navarro, P.; Fernandes,
L.T.; Segales, J.; Garrido, J.J.; Vazquez, J.; Moreno, A.
Quantitative proteomics by 2-DE, 16O/18O labelling and linear ion
trap mass spectrometry analysis of lymph nodes from piglets
inoculated by porcine circovirus type 2. Proteomics, 2011, 11(17),
3452-3469.
[81] Alfonso, P.; Rivera, J.; Hernaez, B.; Alonso, C.; Escribano, J.M.
Identification of cellular proteins modified in response to African
swine fever virus infection by proteomics. Proteomics, 2004, 4(7),
2037-2046.
[82] Sun, J.F.; Shi, Z.X.; Guo, H.C.; Li, S.; Tu, C.C. Proteomic analysis
of swine serum following highly virulent classical swine fever
virus infection. Virol J., 2011, 8, 107.
[83] Tjalsma, H.; Schaeps, R.M.; Swinkels, D.W. Immunoproteomics:
From biomarker discovery to diagnostic applications. Proteomics
Clin. Appl., 2008, 2(2), 167-180.
[84] Martinez-Martinez, S.; Frandoloso, R.; Rodriguez Ferri, E.F.; Gil,
C.; Hernandez-Haro, C.; Yubero, S.; Gutierrez Martin, C.B.
Immunoproteomic analysis of the protective response obtained
with subunit and commercial vaccines against Glasser's disease in
pigs. Vet. Immunol Immunopathol, 2013, 151(3-4), 235-247.
[85] Zhang, W.; Lu, C.P. Immunoproteomics of extracellular proteins of
Chinese virulent strains of Streptococcus suis type 2. Proteomics,
2007, 7(24), 4468-4476.
[86] Wu, Z.; Zhang, W.; Lu, C. Comparative proteome analysis of
secreted proteins of Streptococcus suis serotype 9 isolates from
diseased and healthy pigs. Microb. Pathog., 2008, 45(3), 159-166.
[87] Martins, R.P.; Collado-Romero, M.; Martinez-Gomariz, M.;
Carvajal, A.; Gil, C.; Lucena, C.; Moreno, A.; Garrido, J.J.
Proteomic analysis of porcine mesenteric lymph-nodes after
Salmonella typhimurium infection. J. Proteomics, 2012, 75(14),
4457-4470.
[88] Wang, X.; Ou, D.; Yin, J.; Wu, G.; Wang, J. Proteomic analysis
reveals altered expression of proteins related to glutathione
metabolism and apoptosis in the small intestine of zinc oxide-
supplemented piglets. Amino Acids, 2009, 37(1), 209-218.
[89] Danielsen, M.; Thymann, T.; Jensen, B.B.; Jensen, O.N.; Sangild,
P.T.; Bendixen, E. Proteome profiles of mucosal immunoglobulin
uptake in inflamed porcine gut. Proteomics, 2006, 6(24), 6588-
6596.
[90] Alonso-Fauste, I.; Andres, M.; Iturralde, M.; Lampreave, F.;
Gallart, J.; Alava, M.A. Proteomic characterization by 2-DE in
bovine serum and whey from healthy and mastitis affected farm
animals. J. Proteomics, 2012, 75(10), 3015-3030.
[91] Bradley, A.J.; Leach, K.A.; Breen, J.E.; Green, L.E.; Green, M.J.
Survey of the incidence and aetiology of mastitis on dairy farms in
England and Wales. Vet. Rec., 2007, 160(8), 253-257.
[92] He, Y. Analyses of Brucella pathogenesis, host immunity, and
vaccine targets using systems biology and bioinformatics. Front
Cell Infect Microbiol., 2012, 2, 2.
[93] Pajuaba, A.C.; Silva, D.A.; Almeida, K.C.; Cunha-Junior, J.P.;
Pirovani, C.P.; Camillo, L.R.; Mineo, J.R. Immunoproteomics of
Brucella abortus reveals differential antibody profiles between S19-
vaccinated and naturally infected cattle. Proteomics, 2012, 12(6),
820-831.
[94] Connolly, J.P.; Comerci, D.; Alefantis, T.G.; Walz, A.; Quan, M.;
Chafin, R.; Grewal, P.; Mujer, C.V.; Ugalde, R.A.; DelVecchio,
V.G. Proteomic analysis of Brucella abortus cell envelope and
identification of immunogenic candidate proteins for vaccine
development. Proteomics, 2006, 6(13), 3767-3780.
[95] You, Q.; Verschoor, C.P.; Pant, S.D.; Macri, J.; Kirby, G.M.;
Karrow, N.A. Proteomic analysis of plasma from Holstein cows
testing positive for Mycobacterium avium subsp. paratuberculosis
(MAP). Vet. Immunol Immunopathol, 2012, 148(3-4), 243-251.
[96] Hughes, V.; Garcia-Sanchez, A.; Smith, S.; McLean, K.; Lainson,
A.; Nath, M.; Stevenson, K. Proteome-determined type-specific
proteins of Mycobacterium avium subspecies paratuberculosis. Vet.
Microbiol., 2012, 158(1-2), 153-162.
[97] Weigoldt, M.; Meens, J.; Doll, K.; Fritsch, I.; Mobius, P.; Goethe,
R.; Gerlach, G.F. Differential proteome analysis of Mycobacterium
avium subsp. paratuberculosis grown in vitro and isolated from
cases of clinical Johne's disease. Microbiology, 2011, 157(Pt 2),
557-565.
[98] Cho, D.; Sung, N.; Collins, M.T. Identification of proteins of
potential diagnostic value for bovine paratuberculosis. Proteomics,
2006, 6(21), 5785-5794.
[99] Santema, W.; Overdijk, M.; Barends, J.; Krijgsveld, J.; Rutten, V.;
Koets, A. Searching for proteins of Mycobacterium avium
subspecies paratuberculosis with diagnostic potential by
comparative qualitative proteomic analysis of mycobacterial
tuberculins. Vet. Microbiol., 2009, 138(1-2), 191-196.
[100] Seth, M.; Lamont, E.A.; Janagama, H.K.; Widdel, A.; Vulchanova,
L.; Stabel, J.R.; Waters, W.R.; Palmer, M.V.; Sreevatsan, S.
Biomarker discovery in subclinical mycobacterial infections of
cattle. PLoS One, 2009, 4(5), e5478.
[101] Ammari, M.; McCarthy, F.M.; Nanduri, B.; Pinchuk, L.M.
Analysis of Bovine Viral Diarrhea Viruses-infected monocytes:
identification of cytopathic and non-cytopathic biotype differences.
BMC Bioinformatics, 2010, 11 Suppl 6, S9.
[102] Lee, S.R.; Nanduri, B.; Pharr, G.T.; Stokes, J.V.; Pinchuk, L.M.
Bovine viral diarrhea virus infection affects the expression of
proteins related to professional antigen presentation in bovine
monocytes. Biochim. Biophys. Acta, 2009, 1794(1), 14-22.
[103] Tolboll, T.H.; Danscher, A.M.; Andersen, P.H.; Codrea, M.C.;
Bendixen, E. Proteomics: a new tool in bovine claw disease
research. Vet. J., 2012, 193(3), 694-700.
[104] Xia, C.; Zhang, H.Y.; Wu, L.; Xu, C.; Zheng, J.S.; Yan, Y.J.; Yang,
L.J.; Shu, S. Proteomic analysis of plasma from cows affected with
milk fever using two-dimensional differential in-gel electrophoresis
and mass spectrometry. Res. Vet. Sci., 2012, 93(2), 857-861.
[105] Kuhlers, D.L.; Jungst, S.B.; Marple, D.N.; Rahe, C.H. The effect of
pen density during rearing on subsequent reproductive performance
in gilts. J. Anim. Sci., 1985, 61(5), 1066-1069.
[106] Meunier-Salaun, M.C.; Vantrimponte, M.N.; Raab, A.; Dantzer, R.
Effect of floor area restriction upon performance, behavior and
physiology of growing-finishing pigs. J. Anim. Sci., 1987, 64(5),
1371-1377.
[107] Marco-Ramell, A.; Arroyo, L.; Saco, Y.; Garcia-Heredia, A.;
Camps, J.; Fina, M.; Piedrafita, J.; Bassols, A. Proteomic analysis
reveals oxidative stress response as the main adaptative
physiological mechanism in cows under different production
systems. J. Proteomics, 2012, 75(14), 4399-4411.
[108] Mitchell, G.B.; Clark, M.E.; Siwicky, M.; Caswell, J.L. Stress
alters the cellular and proteomic compartments of bovine
bronchoalveolar lavage fluid. Vet Immunol Immunopathol, 2008,
125(1-2), 111-125.
[109] Xu, C.; Wang, Z. Comparative proteomic analysis of livers from
ketotic cows. Vet. Res. Commun., 2008, 32(3), 263-273.
[110] Kuhla, B.; Kuhla, S.; Rudolph, P.E.; Albrecht, D.; Metges, C.C.
Proteomics analysis of hypothalamic response to energy restriction
in dairy cows. Proteomics, 2007, 7(19), 3602-3617.
[111] Kuhla, B.; Albrecht, D.; Bruckmaier, R.; Viergutz, T.; Nurnberg,
G.; Metges, C.C. Proteome and radioimmunoassay analyses of
pituitary hormones and proteins in response to feed restriction of
dairy cows. Proteomics, 2010, 10(24), 4491-4500.
[112] Daniels, K.M.; Webb, K.E., Jr.; McGilliard, M.L.; Meyer, M.J.;
Van Amburgh, M.E.; Akers, R.M. Effects of body weight and
nutrition on mammary protein expression profiles in Holstein
heifers. J. Dairy Sci., 2006, 89(11), 4276-4288.
[113] Junghans, P.; Beyer, M.; Derno, M.; Petzke, K.J.; Kuchenmeister,
U.; Hennig, U.; Jentsch, W.; Schwerin, M. Studies on persisting
effects of soy-based compared with amino acid-supplemented
casein-based diet on protein metabolism and oxidative stress in
juvenile pigs. Arch. Anim. Nutr., 2007, 61(2), 75-89.
[114] Sarr, O.; Louveau, I.; Kalbe, C.; Metges, C.C.; Rehfeldt, C.;
Gondret, F. Prenatal exposure to maternal low or high protein diets
induces modest changes in the adipose tissue proteome of newborn
piglets. J. Anim. Sci., 2010, 88(5), 1626-1641.
[115] Chae, J.I.; Kim, J.; Lee, S.G.; Koh, M.W.; Jeon, Y.J.; Kim, D.W.;
Ko, S.M.; Seo, K.S.; Lee, H.K.; Choi, N.J.; Cho, S.K.; Ryu, J.;
Kang, S.; Lee, D.S.; Chung, H.M.; Koo, D.B. Quantitative
proteomic analysis of pregnancy-related proteins from peripheral
blood mononuclear cells during pregnancy in pigs. Anim. Reprod.
Sci., 2012, 134(3-4), 164-176.
[116] Gutierrez, A.M.; Miller, I.; Hummel, K.; Nobauer, K.; Martinez-
Subiela, S.; Razzazi-Fazeli, E.; Gemeiner, M.; Ceron, J.J.
Proteomic analysis of porcine saliva. Vet. J., 2011, 187(3), 356-
362.
[117] Lamy, E.; Mau, M. Saliva proteomics as an emerging, non-invasive
tool to study livestock physiology, nutrition and diseases. J.
Proteomics, 2012, 75(14), 4251-4258.
[118] Gutierrez, A.M.; Nobauer, K.; Soler, L.; Razzazi-Fazeli, E.;
Gemeiner, M.; Ceron, J.J.; Miller, I. Detection of potential markers
for systemic disease in saliva of pigs by proteomics: a pilot study.
Vet. Immunol Immunopathol, 2013, 151(1-2), 73-82.
[119] Boehmer, J.L. Proteomic analyses of host and pathogen responses
during bovine mastitis. J. Mammary Gland Biol. Neoplasia, 2011,
16(4), 323-338.
[120] Hogarth, C.J.; Fitzpatrick, J.L.; Nolan, A.M.; Young, F.J.; Pitt, A.;
Eckersall, P.D. Differential protein composition of bovine whey: a
comparison of whey from healthy animals and from those with
clinical mastitis. Proteomics, 2004, 4(7), 2094-2100.
[121] Ibeagha-Awemu, E.M.; Ibeagha, A.E.; Messier, S.; Zhao, X.
Proteomics, genomics, and pathway analyses of Escherichia coli
and Staphylococcus aureus infected milk whey reveal molecular
pathways and networks involved in mastitis. J. Proteome Res.,
2010, 9(9), 4604-4619.
[122] Boehmer, J.L.; DeGrasse, J.A.; McFarland, M.A.; Tall, E.A.;
Shefcheck, K.J.; Ward, J.L.; Bannerman, D.D. The proteomic
advantage: label-free quantification of proteins expressed in bovine
milk during experimentally induced coliform mastitis. Vet.
Immunol Immunopathol, 2010, 138(4), 252-266.
[123] Kim, Y.; Atalla, H.; Mallard, B.; Robert, C.; Karrow, N. Changes
in Holstein cow milk and serum proteins during intramammary
infection with three different strains of Staphylococcus aureus.
BMC Vet. Res., 2011, 7, 51.
[124] Danielsen, M.; Codrea, M.C.; Ingvartsen, K.L.; Friggens, N.C.;
Bendixen, E.; Rontved, C.M. Quantitative milk proteomics--host
responses to lipopolysaccharide-mediated inflammation of bovine
mammary gland. Proteomics, 2010, 10(12), 2240-2249.
[125] Lamy, E.; da Costa, G.; Santos, R.; Capela, E.S.F.; Potes, J.;
Pereira, A.; Coelho, A.V.; Sales Baptista, E. Sheep and goat saliva
proteome analysis: a useful tool for ingestive behavior research?
Physiology & Behavior, 2009, 98(4), 393-401.
[126] Kim, K.; Yang, E.; Vu, G.P.; Gong, H.; Su, J.; Liu, F.; Lu, S. Mass
spectrometry-based quantitative proteomic analysis of Salmonella
enterica serovar Enteritidis protein expression upon exposure to
hydrogen peroxide. BMC Microbiol., 2010, 10, 166.
[127] Newell, D.G.; Koopmans, M.; Verhoef, L.; Duizer, E.; Aidara-
Kane, A.; Sprong, H.; Opsteegh, M.; Langelaar, M.; Threfall, J.;
Scheutz, F.; van der Giessen, J.; Kruse, H. Food-borne diseases -
the challenges of 20 years ago still persist while new ones continue
to emerge. Int. J. Food Microbiol., 2010, 139 Suppl 1, S3-15.
[128] Elmi, A.; Watson, E.; Sandu, P.; Gundogdu, O.; Mills, D.C.; Inglis,
N.F.; Manson, E.; Imrie, L.; Bajaj-Elliott, M.; Wren, B.W.; Smith,
D.G.; Dorrell, N. Campylobacter jejuni outer membrane vesicles
play an important role in bacterial interactions with human
intestinal epithelial cells. Infect Immun., 2012, 80(12), 4089-4098.
[129] Liu, X.; Gao, B.; Novik, V.; Galan, J.E. Quantitative Proteomics of
Intracellular Campylobacter jejuni Reveals Metabolic
Reprogramming. PLoS Pathog., 2012, 8(3), e1002562.
[130] Donaldson, J.R.; Nanduri, B.; Burgess, S.C.; Lawrence, M.L.
Comparative proteomic analysis of Listeria monocytogenes strains
F2365 and EGD. Appl. Environ. Microbiol., 2009, 75(2), 366-373.
[131] Cacace, G.; Mazzeo, M.F.; Sorrentino, A.; Spada, V.; Malorni, A.;
Siciliano, R.A. Proteomics for the elucidation of cold adaptation
mechanisms in Listeria monocytogenes. J. Proteomics, 2010,
73(10), 2021-2030.
[132] Payne, A.; Schmidt, T.B.; Nanduri, B.; Pendarvis, K.; Pittman,
J.R.; Thornton, J.A.; Grissett, J.; Donaldson, J.R. Proteomic
analysis of the response of Listeria monocytogenes to bile salts
under anaerobic conditions. J. Med. Microbiol., 2013, 62(Pt 1), 25-
35.
[133] Soon, J.M.; Chadd, S.A.; Baines, R.N. Escherichia coli O157:H7 in
beef cattle: on farm contamination and pre-slaughter control
methods. Anim. Health Res. Rev., 2011, 12(2), 197-211.
[134] D'Alessandro, A.; Zolla, L. We are what we eat: food safety and
proteomics. J. Proteome Res., 2012, 11(1), 26-36.
[135] Han, M.J.; Lee, S.Y. The Escherichia coli proteome: past, present,
and future prospects. Microbiol. Mol. Biol. Rev., 2006, 70(2), 362-
439.
[136] Sheridan, A.; Lenahan, M.; Condell, O.; Bonilla-Santiago, R.;
Sergeant, K.; Renaut, J.; Duffy, G.; Fanning, S.; Nally, J.E.;
Burgess, C.M. Proteomic and phenotypic analysis of triclosan
tolerant verocytotoxigenic Escherichia coli O157:H19. J.
Proteomics, 2013, 80C, 78-90.
[137] Piras, C.; Soggiu, A.; Bonizzi, L.; Gaviraghi, A.; Deriu, F.; De
Martino, L.; Iovane, G.; Amoresano, A.; Roncada, P. Comparative
proteomics to evaluate multi drug resistance in Escherichia coli.
Mol. Biosyst., 2012, 8(4), 1060-1067.

Received: October 13, 2013 Revised: October 13, 2013 Accepted: November 19, 2013

A Proteomics Perspective From Animal Welfare To Food Safety

Hochgeladen von

Dokumentinformationen

Originalbeschreibung:

Originaltitel

Copyright

Verfügbare Formate

Dieses Dokument teilen

Dokument teilen oder einbetten

Freigabeoptionen

Stufen Sie dieses Dokument als nützlich ein?

Sind diese Inhalte unangemessen?

Copyright:

Verfügbare Formate

A Proteomics Perspective From Animal Welfare To Food Safety

Hochgeladen von

Copyright:

Verfügbare Formate

Send Orders for Reprints to reprints@benthamscience.

Das könnte Ihnen auch gefallen