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

TitleNaturally processed cytokine-derived peptide bound to HLA-class II molecules.
Publication TypeJournal Article
Year of Publication1993
AuthorsHarris PE, Maffei A, Liu Z, Colovai I, Reed EF, Inghirami G, Suciu-Foca N
JournalJ Immunol
Date Published1993 Dec 01
KeywordsAmino Acid Sequence, Base Sequence, Cell Line, Transformed, Cytokines, HLA-DR2 Antigen, HLA-DR5 Antigen, Humans, Lymphocyte Activation, Molecular Sequence Data, Peptides, T-Lymphocytes

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.

Alternate JournalJ Immunol
PubMed ID8245442
Grant ListR01-A125210-06 / / PHS HHS / United States
Related Faculty: 
Giorgio Inghirami, M.D.

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