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The Journal of Immunology, Vol 151, Issue 1 201-210, Copyright © 1993 by American Association of Immunologists

ARTICLES

Differential amino-terminal anchors for peptide binding to H-2M3a or H- 2Kb and H-2Db

SM Shawar, JM Vyas, E Shen, JR Rodgers and RR Rich
Department of Microbiology and Immunology, Baylor College of Medicine, Houston, TX 77030.

We previously established that H-2M3a, the H chain of the maternally transmitted Ag (Mta), is specialized for presentation of N-formylated peptides. We hypothesized that the N-formyl group might prevent or limit the presentation of peptide Ag by H-2K and H-2D molecules. We now show by Mta- and OVA-specific CTL assays, peptide competition, and immunofluorescence analyses that N-formyl modification of four antigenic peptides inhibited their binding by either H-2Kb (OVAMet258- 264, VSVNP52-59, and SVNP324-332) or H2-Db (SVNP324-332, and IVNP366- 374). In contrast, N-formyl-OVAMet258-264 did bind to H2-M3a. The data imply lack of an N-formyl-binding pocket in classical MHC class I molecules and are consistent with a specialized role for H2-M3a in presentation of N-formylated peptides such as derived from intracellular prokaryotic parasites.


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