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Home / Equine Research Bank / Immunogenetics / Peptide-binding motifs of two common equine class I MHC mole...
Immunogenetics2017; 69(5); 351-358; doi: 10.1007/s00251-017-0978-6

Peptide-binding motifs of two common equine class I MHC molecules in Thoroughbred horses.

Abstract: Quantitative peptide-binding motifs of MHC class I alleles provide a valuable tool to efficiently identify putative T cell epitopes. Detailed information on equine MHC class I alleles is still very limited, and to date, only a single equine MHC class I allele, Eqca-1*00101 (ELA-A3 haplotype), has been characterized. The present study extends the number of characterized ELA class I specificities in two additional haplotypes found commonly in the Thoroughbred breed. Accordingly, we here report quantitative binding motifs for the ELA-A2 allele Eqca-16*00101 and the ELA-A9 allele Eqca-1*00201. Utilizing analyses of endogenously bound and eluted ligands and the screening of positional scanning combinatorial libraries, detailed and quantitative peptide-binding motifs were derived for both alleles. Eqca-16*00101 preferentially binds peptides with aliphatic/hydrophobic residues in position 2 and at the C-terminus, and Eqca-1*00201 has a preference for peptides with arginine in position 2 and hydrophobic/aliphatic residues at the C-terminus. Interestingly, the Eqca-16*00101 motif resembles that of the human HLA A02-supertype, while the Eqca-1*00201 motif resembles that of the HLA B27-supertype and two macaque class I alleles. It is expected that the identified motifs will facilitate the selection of candidate epitopes for the study of immune responses in horses.
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Publication Date: 2017-03-18 PubMed ID: 28315936PubMed Central: PMC5555743DOI: 10.1007/s00251-017-0978-6Google Scholar: Lookup
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  • N.I.H.
  • Extramural
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  • Non-U.S. Gov't

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research focuses on the discovery and quantitative analysis of peptide-binding motifs for two more equine Major Histocompatibility Complex (MHC) class I alleles common in Thoroughbred horses, providing valuable information towards the identification of T cell epitopes which may be key in studying immune responses in horses.

Understanding MHC Class I Alleles & Their Significance

  • The Major Histocompatibility Complex (MHC) class I alleles are vital components in the immune response system of vertebrates, including horses. They play a crucial role in recognizing foreign substances, presenting them to T cells, and triggering an immune response.
  • Thus, understanding the peptide-binding motifs of these MHC class I alleles provides an efficient way to identify putative T cell epitopes – potential targets of the T cell immune response.

Extension of Characterized ELA Class I Specificities

  • Prior to this study, only one equine MHC class I allele (Eqca-1*00101 of the ELA-A3 haplotype) was known.
  • This research extends that knowledge by identifying and quantifying the peptide-binding motifs of two more alleles – Eqca-16*00101 (ELA-A2) and Eqca-1*00201 (ELA-A9), both prevalent in Thoroughbred horses.
  • These findings allow for a broader understanding of equine immune responses.

Methods and Findings of the Study

  • The study utilised analyses of endogenously bound and eluted ligands alongside the screening of positional scanning combinatorial libraries to derive detailed and quantitative peptide-binding motifs for both alleles.
  • The study revealed that Eqca-16*00101 preferentially binds peptides with aliphatic/hydrophobic residues in position 2 and at the C-terminus.
  • Eqca-1*00201, on the other hand, has a preference for peptides with arginine in position 2 and hydrophobic/aliphatic residues at the C-terminus.
  • Interestingly, the Eqca-16*00101 motif shows resemblance to that of the human HLA A02-supertype, while the Eqca-1*00201 motif is similar to the HLA B27-supertype and two macaque class I alleles.

Implications of the Study

  • The identified motifs provide valuable insight into the immune response mechanisms in horses.
  • This will facilitate the selection of candidate epitopes for further study and understanding of immune responses in horses, potentially opening new pathways for disease prevention and treatment in the equine industry.

Cite This Article

APA
Bergmann T, Lindvall M, Moore E, Moore E, Sidney J, Miller D, Tallmadge RL, Myers PT, Malaker SA, Shabanowitz J, Osterrieder N, Peters B, Hunt DF, Antczak DF, Sette A. (2017). Peptide-binding motifs of two common equine class I MHC molecules in Thoroughbred horses. Immunogenetics, 69(5), 351-358. https://doi.org/10.1007/s00251-017-0978-6

Publication

Immunogenetics
ISSN: 1432-1211
NlmUniqueID: 0420404
Country: United States
Language: English
Volume: 69
Issue: 5
Pages: 351-358

Researcher Affiliations

Bergmann, Tobias
  • Institut für Virologie, Freie Universität Berlin, 14163, Berlin, Germany.
Lindvall, Mikaela
  • Department of Vaccine Discovery, La Jolla Institute for Allergy and Immunology, 9420 Athena Circle, La Jolla, CA, 92037, USA.
Moore, Erin
  • Department of Vaccine Discovery, La Jolla Institute for Allergy and Immunology, 9420 Athena Circle, La Jolla, CA, 92037, USA.
Moore, Eugene
  • Department of Vaccine Discovery, La Jolla Institute for Allergy and Immunology, 9420 Athena Circle, La Jolla, CA, 92037, USA.
Sidney, John
  • Department of Vaccine Discovery, La Jolla Institute for Allergy and Immunology, 9420 Athena Circle, La Jolla, CA, 92037, USA.
Miller, Donald
  • Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY, 14853, USA.
Tallmadge, Rebecca L
  • Department of Clinical Sciences, College of Veterinary Medicine, Cornell University, Ithaca, NY, 14853, USA.
Myers, Paisley T
  • Department of Chemistry, University of Virginia, Charlottesville, VA, 22904, USA.
Malaker, Stacy A
  • Department of Chemistry, University of Virginia, Charlottesville, VA, 22904, USA.
Shabanowitz, Jeffrey
  • Department of Chemistry, University of Virginia, Charlottesville, VA, 22904, USA.
Osterrieder, Nikolaus
  • Institut für Virologie, Freie Universität Berlin, 14163, Berlin, Germany.
Peters, Bjoern
  • Department of Vaccine Discovery, La Jolla Institute for Allergy and Immunology, 9420 Athena Circle, La Jolla, CA, 92037, USA.
Hunt, Donald F
  • Department of Chemistry, University of Virginia, Charlottesville, VA, 22904, USA.
  • Department of Pathology, University of Virginia, Charlottesville, VA, 22908, USA.
Antczak, Douglas F
  • Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY, 14853, USA.
Sette, Alessandro
  • Department of Vaccine Discovery, La Jolla Institute for Allergy and Immunology, 9420 Athena Circle, La Jolla, CA, 92037, USA. alex@lji.org.

MeSH Terms

  • Amino Acid Motifs
  • Animals
  • Epitopes, T-Lymphocyte / immunology
  • Genes, MHC Class I
  • Haplotypes
  • Histocompatibility Antigens Class I / immunology
  • Histocompatibility Antigens Class I / metabolism
  • Horses
  • Peptide Fragments / immunology
  • Peptide Fragments / metabolism
  • Protein Binding
  • Protein Domains

Grant Funding

  • R38 AI140299 / NIAID NIH HHS
  • U19 AI090023 / NIAID NIH HHS
  • R01 AI112566 / NIAID NIH HHS
  • HHSN272200900042C / NIAID NIH HHS
  • R37 AI033993 / NIAID NIH HHS
  • HHSN272201400045C / NIAID NIH HHS
  • R01 AI033993 / NIAID NIH HHS

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Citations

This article has been cited 1 times.
  1. Vasoya D, Tzelos T, Benedictus L, Karagianni AE, Pirie S, Marr C, Oddsdóttir C, Fintl C, Connelley T. High-Resolution Genotyping of Expressed Equine MHC Reveals a Highly Complex MHC Structure.. Genes (Basel) 2023 Jul 10;14(7).
    doi: 10.3390/genes14071422pubmed: 37510326google scholar: lookup
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