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The Journal of Immunology, Vol 151, Issue 11 5975-5983, Copyright © 1993 by American Association of Immunologists

ARTICLES

Naturally processed cytokine-derived peptide bound to HLA-class II molecules

PE Harris, A Maffei, Z Liu, I Colovai, EF Reed, G Inghirami and N Suciu-Foca
College of Physicians and Surgeons of Columbia University, Department of Pathology, New York, NY 10032.

Sequence analysis of HLA-class II (HLA-DR beta 1-1502 and 1104)-bound self-peptides from a transformed B cell line was performed. The sequences of naturally processed self-peptides bound to HLA-DR2 and DR5 were compared with protein and nucleic acid data bases for homology to known precursor proteins. Of the matches to known precursors, one peptide showed 100% homology to the third framework and CDR3 regions of Ig VH expressed by the line. Another peptide matched 100% to the human equivalent of macrophage inflammatory protein (MIP). A synthetic peptide corresponding to the naturally processed form of MIP (KPGVIFLTKRSRQV) was shown to inhibit Ag-specific HLA-DR beta 1*1104- restricted T cell proliferation. This indicates that the MIP peptide binds to HLA-DR beta 1*1104. The MIP peptide belongs to a set of peptides that showed uniform NH2-terminal processing. In this set, proline always occurred as the second residue followed by a basic lysine or arginine in position nine. This suggests that final NH2- terminal processing of peptides precedes their binding to MHC molecules. A distinct, second set of peptides showed ragged NH2- terminii, as has been reported for other naturally processed MHC-class II-bound self-peptides.


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