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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.
Author(s): von Delvig A, Robinson JH
Publication type: Article
Publication status: Published
Journal: Journal of Biological Chemistry
Print publication date: 06/02/1998
ISSN (print): 0021-9258
ISSN (electronic): 1083-351X
Publisher: American Society for Biochemistry and Molecular Biology, Inc.
PubMed id: 9452445
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