Special Issue "Proteomics in Veterinary Research and Zoonotic Diseases"

A special issue of Animals (ISSN 2076-2615). This special issue belongs to the section "Animal Genetics and Genomics".

Deadline for manuscript submissions: closed (31 December 2021) | Viewed by 12926

Special Issue Editors

Dr. Alessio Soggiu
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Guest Editor
Department of Veterinary Medicine, University of Milan, via Celoria 10, 20133 Milan, Italy
Interests: proteomics of host-pathogen interaction in animal models of infection; Metaproteomics/microbiota; bacterial competition in food and in biological fluids; Zoonotic and infectious diseases; immunoproteomics
Special Issues, Collections and Topics in MDPI journals
Dr. Cristian Piras
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Guest Editor
Department of Chemistry, University of Reading Whiteknights, Reading RG6 6AD, UK
Interests: proteomics of antibiotic resistant bacteria isolated from animals; fast profiling by mass spectrometry of animal welfare in food and in biological fluids; resistome analysis; protein markers of metabolic disorders and fertility.

Special Issue Information

Dear Colleagues,

Proteomics allows the full characterization of protein content in complex matrices. A tissue or a biological fluid can represent the matrix, and it is possible to uncover the nature, relative abundance, and related post-translational modifications of such a dynamic proteome. Technological innovations in electrophoresis, chromatography, and mass spectrometry lead to the development of wider applications of proteomics.

The application of proteomics to veterinary medicine is able to simultaneously provide important information about the modulation of thousands of proteins and to define cause–effect relationships between expression and post-translational modifications of proteins in healthy and diseased conditions. Moreover, it can be used to rapidly assess animal welfare through fast profiling, to evaluate food safety in animal products, and to investigate the complex relationship between the host and the pathogenic or nonpathogenic microbial communities.

In the light of these premises, we invite investigators to provide their contributions under the form of review articles or original research articles. The main topic will be related to proteomics applications in the field of veterinary medicine, including in vitro and in vivo systems. The final aim is to provide a collection of contributions to the knowledge in veterinary medicine on the topic of proteomics.

Dr. Alessio Soggiu
Dr. Cristian Piras
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Animals is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Proteomics
  • immunoproteomics
  • Infectious diseases
  • Veterinary medicine
  • Zoonosis
  • Food of animal origin
  • Diagnostics
  • Animal health and welfare
  • Microbiota and microbial communities

Published Papers (8 papers)

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Research

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Article
Insect Protein-Based Diet as Potential Risk of Allergy in Dogs
Animals 2021, 11(7), 1942; https://doi.org/10.3390/ani11071942 - 29 Jun 2021
Cited by 10 | Viewed by 1876
Abstract
Before insects can be used widely as an alternative source of dietary protein, their allerginicity should be investigated. Therefore, the aim of our study was to assess the potential adverse reactions of the immune system of dogs against Tenebrio molitor proteins. Dogs sensitised [...] Read more.
Before insects can be used widely as an alternative source of dietary protein, their allerginicity should be investigated. Therefore, the aim of our study was to assess the potential adverse reactions of the immune system of dogs against Tenebrio molitor proteins. Dogs sensitised to storage mites T. putrescentiae and A. siro were included. Clinically healthy and clinically allergic dogs were compared. Proteins were extracted from mealworm larvae and their digestibility determined by in vitro incubation with digestive proteases. Mealworm protein extracts and digests were analysed by SDS–PAGE. Canine sera tested for the presence of mite-specific IgEs were used for subsequent Western blotting. LC-MS/MS analysis was used to identify mealworm proteins and their allergenic potential was predicted with the AllermatchTM tool. The binding of canine sera IgEs to mealworm proteins was confirmed; however, the differences between the two groups of dogs were not significant. Moreover, no clear correlation was found between sensitisation to storage mites and clinical status of the dogs. Altogether, 17 different proteins were identified, including tropomyosin, α-amylase, and Tm-E1a cuticular protein that are known cross-reacting IgE-binding allergens. Our results suggest that dogs allergic to mites may clinically express also the cross-reactivity with mealworm proteins. Full article
(This article belongs to the Special Issue Proteomics in Veterinary Research and Zoonotic Diseases)
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Article
Tandem Mass Tag (TMT) Proteomic Analysis of Saliva in Horses with Acute Abdominal Disease
Animals 2021, 11(5), 1304; https://doi.org/10.3390/ani11051304 - 30 Apr 2021
Cited by 2 | Viewed by 1162
Abstract
The aim of this study was to investigate the changes in the salivary proteome in horses with acute abdominal disease (AAD) using a tandem mass tags (TMT)-based proteomic approach. The saliva samples from eight horses with AAD were compared with six healthy horses [...] Read more.
The aim of this study was to investigate the changes in the salivary proteome in horses with acute abdominal disease (AAD) using a tandem mass tags (TMT)-based proteomic approach. The saliva samples from eight horses with AAD were compared with six healthy horses in the proteomic study. Additionally, saliva samples from eight horses with AAD and eight controls were used to validate lactoferrin (LF) in saliva. The TMT analysis quantified 118 proteins. Of these, 17 differed significantly between horses with AAD and the healthy controls, 11 being downregulated and 6 upregulated. Our results showed the downregulation of gamma-enteric smooth muscle actin (ACTA2), latherin isoform X1, and LF. These proteins could be closely related to an impaired primary immune defense and antimicrobial capacity in the mucosa. In addition, there was an upregulation of mucin 19 (MUC19) and the serine protease inhibitor Kazal-type 5 (SPINK5) associated with a protective effect during inflammation. The proteins identified in our study could have the potential to be novel biomarkers for diagnosis or monitoring the physiopathology of the disease, especially LF, which decreased in the saliva of horses with AAD and was successfully measured using a commercially available immunoassay. Full article
(This article belongs to the Special Issue Proteomics in Veterinary Research and Zoonotic Diseases)
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Article
Proteomic Analysis of the Secretome and Exosomes of Feline Adipose-Derived Mesenchymal Stem Cells
Animals 2021, 11(2), 295; https://doi.org/10.3390/ani11020295 - 24 Jan 2021
Cited by 4 | Viewed by 1664
Abstract
Mesenchymal stem cells (MSCs) have been shown to have therapeutic efficacy in different complex pathologies in feline species. This effect is attributed to the secretion of a wide variety of bioactive molecules and extracellular vesicles, such as exosomes, with significant paracrine activity, encompassed [...] Read more.
Mesenchymal stem cells (MSCs) have been shown to have therapeutic efficacy in different complex pathologies in feline species. This effect is attributed to the secretion of a wide variety of bioactive molecules and extracellular vesicles, such as exosomes, with significant paracrine activity, encompassed under the concept of the secretome. However, at present, the exosomes from feline MSCs have not yet been studied in detail. The objective of this study is to analyze and compare the protein profiles of the secretome as a whole and its exosomal fraction from feline adipose-derived MSCs (fAd-MSCs). For this, Gene Ontology (GO), Kyoto Encyclopedia of Genes and Genomes (KEGG) and Protein–Protein Interaction Networks Functional Enrichment Analysis (STRING) were utilized. A total of 239 proteins were identified in the secretome, and 228 proteins specific to exosomes were identified, with a total of 133 common proteins. The proteins identified in the secretome were located in the extracellular regions and in the cytoplasm, while the exosomal proteins were located mainly in the membrane, cytoplasm and cytosol. Regarding function, in the secretome, proteins involved in different metabolic pathways, in pathways related to the immune system and the endocrine system and in the processing of proteins in the endoplasmic reticulum predominated. In contrast, proteins specific to exosomes were predominantly associated with endocytosis, cell junctions, platelet activation and other cell signaling pathways. The possible future use of the secretome, or some of its components, such as exosomes, would provide a non-cell-based therapeutic strategy for the treatment of different diseases that would avoid the drawbacks of cell therapy. Full article
(This article belongs to the Special Issue Proteomics in Veterinary Research and Zoonotic Diseases)
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Article
Effects of Different Dietary Vegetable Lipid Sources on Health Status in Nile Tilapia (Oreochromis niloticus): Haematological Indices, Immune Response Parameters and Plasma Proteome
Animals 2020, 10(8), 1377; https://doi.org/10.3390/ani10081377 - 08 Aug 2020
Cited by 8 | Viewed by 1048
Abstract
This study aimed to investigate the effects of DLs, including palm oil (PO; an SFAs), linseed oil (LO; n-3 PUFAs) and soybean oil (SBO; n-6 PUFAs) on the health status of Nile tilapia (Oreochromis niloticus) during adulthood. Three experimental diets incorporating [...] Read more.
This study aimed to investigate the effects of DLs, including palm oil (PO; an SFAs), linseed oil (LO; n-3 PUFAs) and soybean oil (SBO; n-6 PUFAs) on the health status of Nile tilapia (Oreochromis niloticus) during adulthood. Three experimental diets incorporating PO, LO or SBO were fed to adult Nile tilapia for a period of 90 days, and haematological and innate immune parameters were evaluated. Proteome analysis was also conducted to evaluate the effects of DLs on plasma proteins. The tested DLs had no significant effects on red blood cell (RBC) count, haematocrit, haemoglobin, and total immunoglobulin and lysozyme activity. Dietary LO led to increased alternative complement 50 activity (ACH50), and proteome analysis revealed that PO and SBO enhanced A2ML, suggesting that different DLs promote immune system via different processes. Dietary LO or SBO increased the expression of several proteins involved in coagulation activity such as KNG1, HRG and FGG. Increased HPX in fish fed with PO suggests that SFAs are utilised in heme lipid-oxidation. Overall, DLs with distinct fatty acids (FAs) affect several parameters corresponding to health status in Nile tilapia, and dietary LO and SBO seemed to strengthen health in this species. Full article
(This article belongs to the Special Issue Proteomics in Veterinary Research and Zoonotic Diseases)
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Article
Proteomic Analysis of Fresh and Liquid-Stored Boar Spermatozoa
Animals 2020, 10(4), 553; https://doi.org/10.3390/ani10040553 - 26 Mar 2020
Cited by 3 | Viewed by 1311
Abstract
In this study comparative proteomics was used to define changes in the expression of the spermatozoa proteins during liquid storage. Semen from eight boars was analyzed on the day of collection and after liquid preservation at 15–17 °C for three days. Sperm parameters [...] Read more.
In this study comparative proteomics was used to define changes in the expression of the spermatozoa proteins during liquid storage. Semen from eight boars was analyzed on the day of collection and after liquid preservation at 15–17 °C for three days. Sperm parameters (concentration, motility, morphology, vitality) and percentage of non-capacitated and acrosomal-reacted spermatozoa were determined. Sperm proteins were extracted and separated by two-dimensional sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and proteomic profiles were computationally compared to highlight differentially expressed protein spots that were, in turn, identified by mass spectrometry. The intensities of four spots were significantly different between fresh and liquid stored sperm. Namely: ATP citrate lyase, chaperonin containing T-complex polypeptide 1 (TCP1) subunit ε and probable phospholipid-transporting ATP-ase were over-expressed in liquid stored sperm, whereas cytosolic non-specific dipeptidase was over-expressed in fresh sperm. These differentially expressed proteins could be used as plausible biomarkers for the evaluation of boar semen quality and spermatozoa survival after liquid storage and could help to address problems associated with sperm preservation. Full article
(This article belongs to the Special Issue Proteomics in Veterinary Research and Zoonotic Diseases)
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Article
Proteomic Analysis of Beef Tenderloin and Flank Assessed Using an Isobaric Tag for Relative and Absolute Quantitation (iTRAQ)
Animals 2020, 10(1), 150; https://doi.org/10.3390/ani10010150 - 16 Jan 2020
Cited by 1 | Viewed by 1258
Abstract
Herein, we performed a proteomic analysis of tenderloin and flank steaks from Simmental cattle using the isobaric tags for a relative and absolute quantification (iTRAQ) approach. We identified 17 amino acids in both steaks, and Gly, Cys, Ile, Lys, and Pro differed most [...] Read more.
Herein, we performed a proteomic analysis of tenderloin and flank steaks from Simmental cattle using the isobaric tags for a relative and absolute quantification (iTRAQ) approach. We identified 17 amino acids in both steaks, and Gly, Cys, Ile, Lys, and Pro differed most in abundance between the steak types (p < 0.05). A comparison of the expression patterns in steaks revealed 128 differentially expressed proteins (DEPs), of which 44 were up-regulated and 84 were down-regulated. Furthermore, 27 DEPs (p < 0.05) were subjected to gene ontology (GO) analysis, and many were found to be related to oxidation-reduction, metabolism, hydrogen ion transmembrane transport, transport, the tricarboxylic acid (TCA) cycle, mitochondrial electron transport, and the conversion of nicotinamide adenine dinucleotide (NADH) to ubiquinone. Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analysis also implicated these DEPs in various signalling pathways, including oxidative phosphorylation, cardiac muscle contraction, the TCA cycle, biosynthesis, and the metabolism. These findings provide a new insight into key proteins involved in the determination of amino acid composition in beef. Full article
(This article belongs to the Special Issue Proteomics in Veterinary Research and Zoonotic Diseases)
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Article
Unraveling the Adipose Tissue Proteome of Transition Cows through Severe Negative Energy Balance
Animals 2019, 9(12), 1013; https://doi.org/10.3390/ani9121013 - 21 Nov 2019
Cited by 5 | Viewed by 1903
Abstract
Fat mobilization in high-yielding dairy cows during early lactation occurs to overcome negative energy balance (NEB), caused by insufficient feed intake and the concomitant increased nutritional requirements. For this reason, adipose tissue represents an essential organ for healthy and performant lactation. However, only [...] Read more.
Fat mobilization in high-yielding dairy cows during early lactation occurs to overcome negative energy balance (NEB), caused by insufficient feed intake and the concomitant increased nutritional requirements. For this reason, adipose tissue represents an essential organ for healthy and performant lactation. However, only a few data are known about adipose tissue proteome and its metabolic status during peripartum. The aim of this study was to analyze the differential proteomics profiles of subcutaneous adipose tissue belonging to cows with different NEB scores (low NEB and severe NEB). Both groups were analyzed at three different time points (one month before calving, one and sixteen weeks after calving) that were related to different levels and rates of adipose tissue mobilization. The dataset highlighted the differential expression of the same four key proteins (annexin A2, actin-related protein 10, glyceraldehyde-3-phosphate dehydrogenase, and fatty acid-binding protein) involved in lipid metabolism during all time points and of other 22 proteins typical of the other comparisons among remaining time points. The obtained dataset suggested that the individual variability in adipose tissue metabolism/mobilization/energy availability could be linked to the different outcomes in levels of energy balance and related physical complications among dairy cows during peripartum. Full article
(This article belongs to the Special Issue Proteomics in Veterinary Research and Zoonotic Diseases)
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Review

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Review
Toxoplasma gondii Recombinant Antigens in the Serodiagnosis of Toxoplasmosis in Domestic and Farm Animals
Animals 2020, 10(8), 1245; https://doi.org/10.3390/ani10081245 - 22 Jul 2020
Cited by 10 | Viewed by 1615
Abstract
Toxoplasmosis is caused by an intracellular protozoan, Toxoplasma gondii, and is a parasitic disease that occurs in all warm-blooded animals, including humans. Toxoplasmosis is one of the most common parasitic diseases of animals and results in reproductive losses. Toxoplasmosis in humans is [...] Read more.
Toxoplasmosis is caused by an intracellular protozoan, Toxoplasma gondii, and is a parasitic disease that occurs in all warm-blooded animals, including humans. Toxoplasmosis is one of the most common parasitic diseases of animals and results in reproductive losses. Toxoplasmosis in humans is usually caused by eating raw or undercooked meat or consuming dairy products containing the parasite. Diagnosis of toxoplasmosis is currently based on serological assays using native antigens to detect specific anti-T. gondii antibodies. Due to the high price, the available commercial agglutination assays are not suited to test a large number of animal serum samples. The recent development of proteomics elucidated the antigenic structure of T. gondii and enabled the development of various recombinant antigens that can be used in new, cheaper, and more effective diagnostic tools. Continuous development of scientific disciplines, such as molecular biology and genetic engineering, allows for the production of new recombinant antigens and provides the basis for new diagnostic tests for the detection of anti-T. gondii antibodies in animal serum samples. Full article
(This article belongs to the Special Issue Proteomics in Veterinary Research and Zoonotic Diseases)
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