Differential amino-terminal anchors for peptide binding to H-2M3a or H-2Kb and H-2Db
| Autor: | S M Shawar, J M Vyas, E Shen, J R Rodgers, R R Rich |
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| Rok vydání: | 1993 |
| Předmět: | |
| Zdroj: | The Journal of Immunology. 151:201-210 |
| ISSN: | 1550-6606 0022-1767 |
| DOI: | 10.4049/jimmunol.151.1.201 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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