Characterization of the peptide-binding specificity of the chimpanzee class I alleles A 0301 and A 0401 using a combinatorial peptide library.
Chimpanzees represent important models for studying several human pathogens. In the present study, we utilized a combinatorial peptide library to characterize the binding specificities of the chimpanzee class I molecules Patr A 0301 and A 0401, both of which are present in about 17% of chimpanzees. Patr A 0301 was found to recognize peptides using the canonical position 2/C-terminus spacing, with the small residues S, T, and A being the most preferred in position 2, and the positively charged residues R and K preferred at the C terminus. Patr A 0401 was found to recognize a more complex motif where the C terminus and then the residue in positions 1 and/or 5 are the primary anchors. Like A 0301, the C-terminal preference of A 0401 is for positively charged residues. At positions 1 and 5, positively charged and large residues are the most preferred, respectively. Coefficient values derived from the combinatorial library proved to be an efficient means for predicting A 0301 and A 0401 binders. The present data provide detailed information to facilitate the identification of potential T cell epitopes recognized in the context of two common chimpanzee class I alleles, and further validate the combinatorial library approach as an efficient method to characterize class I binding specificities.
Sidney
John
J
La Jolla Institute for Allergy and Immunology, 9420 Athena Circle, La Jolla, CA 92037, USA.
Peters
Bjoern
B
Moore
Carrie
C
Pencille
Timothy J
TJ
Ngo
Sandy
S
Masterman
Kelly-Anne
KA
Asabe
Shinichi
S
Pinilla
Clemencia
C
Chisari
Francis V
FV
Sette
Alesandro
A
D000483:Alleles; D000818:Animals; D015395:Histocompatibility Antigens Class I / Q000235:genetics / Q000276:immunology*; D002679:Pan troglodytes / Q000276:immunology*; D019151:Peptide Library; D011485:Protein Binding
D015395:Histocompatibility Antigens Class I; D019151:Peptide Library
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