Peptide-binding motifs of two common equine class I MHC molecules in Thoroughbred horses.
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.
Institut für Virologie, Freie Universität Berlin, 14163, Berlin, Germany.
Tobias
T
Bergmann
Department of Vaccine Discovery, La Jolla Institute for Allergy and Immunology, 9420 Athena Circle, La Jolla, CA, 92037, USA.
Mikaela
M
Lindvall
Department of Vaccine Discovery, La Jolla Institute for Allergy and Immunology, 9420 Athena Circle, La Jolla, CA, 92037, USA.
Erin
E
Moore
Department of Vaccine Discovery, La Jolla Institute for Allergy and Immunology, 9420 Athena Circle, La Jolla, CA, 92037, USA.
Eugene
E
Moore
Department of Vaccine Discovery, La Jolla Institute for Allergy and Immunology, 9420 Athena Circle, La Jolla, CA, 92037, USA.
John
J
Sidney
Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY, 14853, USA.
Donald
D
Miller
Department of Clinical Sciences, College of Veterinary Medicine, Cornell University, Ithaca, NY, 14853, USA.
Rebecca L
RL
Tallmadge
Department of Chemistry, University of Virginia, Charlottesville, VA, 22904, USA.
Paisley T
PT
Myers
Department of Chemistry, University of Virginia, Charlottesville, VA, 22904, USA.
Stacy A
SA
Malaker
Department of Chemistry, University of Virginia, Charlottesville, VA, 22904, USA.
Jeffrey
J
Shabanowitz
Institut für Virologie, Freie Universität Berlin, 14163, Berlin, Germany.
Nikolaus
N
Osterrieder
Department of Vaccine Discovery, La Jolla Institute for Allergy and Immunology, 9420 Athena Circle, La Jolla, CA, 92037, USA.
Bjoern
B
Peters
Department of Chemistry, University of Virginia, Charlottesville, VA, 22904, USA.|Department of Pathology, University of Virginia, Charlottesville, VA, 22908, USA.
Donald F
DF
Hunt
Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY, 14853, USA.
Douglas F
DF
Antczak
Department of Vaccine Discovery, La Jolla Institute for Allergy and Immunology, 9420 Athena Circle, La Jolla, CA, 92037, USA. alex@lji.org.
Alessandro
A
Sette
D020816:Amino Acid Motifs; D000818:Animals; D018984:Epitopes, T-Lymphocyte / Q000276:immunology*; D005805:Genes, MHC Class I; D006239:Haplotypes; D015395:Histocompatibility Antigens Class I / Q000276:immunology / Q000378:metabolism*; D006736:Horses; D010446:Peptide Fragments / Q000276:immunology / Q000378:metabolism*; D011485:Protein Binding; D000072417:Protein Domains
D018984:Epitopes, T-Lymphocyte; D015395:Histocompatibility Antigens Class I; D010446:Peptide Fragments
Equus caballus (Eqca); MHC binding motif; MHC class I; Peptide binding; T cell epitope