The Journal of Experimental Medicine
VeriKine-HS Human IFN-Beta
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© The Rockefeller University Press, 0022-1007/1997/1/367/ $5.00
The Journal of Experimental Medicine, Volume 185, Number 2, January 20, 1997 367-372

Brief Definitive Reports

HLA Class I Binding Motifs Derived from Random Peptide Libraries Differ at the COOH Terminus from Those of Eluted Peptides

Miles P. Davenport*, Katherine J. Smith*, Dan Barouch*, Scott W. Reid*, Wanda M. Bodnar§, Anthony C. Willis{ddagger}, Donald F. Hunt§, and Adrian V.S. Hill*

From the * Molecular Immunology Group, Institute of Molecular Medicine, Nuffield Department of Medicine, University of Oxford, John Radcliffe Hospital, Headington, OX3 9DU, United Kingdom; {ddagger} Medical Research Council Immunochemistry Unit, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom; and the § Department of Chemistry, University of Virginia, Charlottesville, Virginia 22903

Recombinant HLA-A2, HLA-B8, or HLA-B53 heavy chain produced in Escherichia coli was combined with recombinant β2-microglobulin (β2m) and a pool of randomly synthesised nonamer peptides. This mixture was allowed to refold to form stable major histocompatability complex (MHC) class I complexes, which were then purified by gel filtration chromatography. The peptides bound to the MHC class I molecules were subsequently eluted and sequenced as a pool. Peptide binding motifs for these three MHC class I molecules were derived and compared with previously described motifs derived from analysis of naturally processed peptides eluted from the surface of cells. This comparison indicated that the peptides bound by the recombinant MHC class I molecules showed a similar motif to naturally processed and presented peptides, with the exception of the peptide COOH terminus. Whereas the motifs derived from naturally processed peptides eluted from HLA-A2 and HLA-B8 indicated a strong preference for hydrophobic amino acids at the COOH terminus, this preference was not observed in our studies. We propose that this difference reflects the effects of processing or transport on the peptide repertoire available for binding to MHC class I molecules in vivo.

Address correspondence to Miles P. Davenport, Molecular Immunology Group, Institute of Molecular Medicine, Nuffield Department of Medicine, University of Oxford, John Radcliffe Hospital, Headington, OX3 9DU, UK.

Thanks to H. Reyburn for helpful comments.

M.P. Davenport is supported by the Lionel Murphy Foundation and the Wellcome Trust. A.V.S. Hill is a Wellcome Trust Principal Research Fellow. D. Barouch is supported by a Marshall Scholarship.


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