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Different endosomal proteolysis requirements for antigen processing of two T-cell epitopes of the M5 protein from viable Streptococcus pyogenes

Lookup NU author(s): Dr Alexei von Delwig, Professor John Robinson


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We studied endosomal proteolysis of the surface fibrillar M5 protein from viable Streptococcus pyogenes as an essential step involved in major histocompatibility complex class II-restricted antigen processing of two immunodominant CD4+ T-cell epitopes (17-31/E(d) and 308-319/A(d)). Intracellular proteolysis of viable streptococci for presentation of 17-31, bound by serine proteinase cleavage sites, was mediated by serine proteinases, whereas processing of soluble recombinant M5 protein required in addition cysteine proteinases. Furthermore, processing of 17-31 was resistant to ammonium chloride and thus was not dependent on endosome acidification. Cysteine and serine proteinase cleavage sites were located adjacent to 308- 319, and its processing was dependent on serine, cysteine, and aspartic proteinases, as well as on endosomal acidification. The data suggest that antigen processing of two major T-cell epitopes on streptococcal M5 protein occurred in different endosomal compartments by different classes of intracellular proteinases.

Publication metadata

Author(s): von Delvig A, Robinson JH

Publication type: Article

Publication status: Published

Journal: Journal of Biological Chemistry

Year: 1998

Volume: 273

Issue: 6

Pages: 3291-3295

Print publication date: 06/02/1998

ISSN (print): 0021-9258

ISSN (electronic): 1083-351X

Publisher: American Society for Biochemistry and Molecular Biology, Inc.


DOI: 10.1074/jbc.273.6.3291

PubMed id: 9452445


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