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Identification of Five Different Patr Class I Molecules That Bind HLA Supertype Peptides and Definition of Their Peptide Binding Motifs¹

Denise M. McKinney^2,*, Ann L. Erickson, Christopher M. Walker, Robert Thimme, Francis V. Chisari, John Sidney^* and Alessandro Sette^*

^* Epimmune Inc., San Diego, CA 92121; Children’s Research Institute and The Ohio State University, Columbus, OH 43205; and The Scripps Research Institute, La Jolla, CA 92037

We have sequenced the Pan troglodytes class I (Patr) molecules from three common chimpanzees and expressed them as single molecules in a class I-deficient cell line. These lines were utilized to obtain purified class I molecules to define the peptide binding motifs associated with five different Patr molecules. Based on these experiments, as well as analysis of the predicted structure of the B and F polymorphic MHC pockets, we classified five Patr molecules (Patr-A*0101, Patr-B*0901, Patr-B*0701, Patr-A*0602, and Patr-B*1301) within previously defined supertype specificities associated with HLA class I molecules (HLA-A3, -B7, -A1, and -A24 supertypes). The overlap in the binding repertoire between specific HLA and Patr class I molecules was in the range of 33 to 92%, depending on the particular Patr molecule as assessed by the binding of HIV-, hepatitis B virus-, and hepatitis C virus-derived epitopes. Finally, live cell binding assays of nine chimpanzee-derived B cell lines demonstrated that HLA supertype peptides bound to Patr class I molecules with frequencies in the 20–50% range.

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