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- W2105269145 abstract "The streptococcal pyrogenic exotoxin B (SpeB) is an important virulence factor of group A streptococci (GAS) with cysteine protease activity. Maturation of SpeB to a proteolytically active form was suggested to be dependent on cell-wall-anchored M1 protein, the major surface protein of GAS (M. Collin and A. Olsen, Mol. Microbiol. 36:1306-1318, 2000). Collin and Olsen showed that mutant GAS strains expressing truncated M protein secrete a conformationally different form of unprocessed SpeB with no proteolytic activity. Alternatively, we hypothesized that a truncated M protein may interfere with processing of this secreted protease, and therefore we tested cysteine protease activity in genetically defined mutant strains that express either no M protein or membrane-anchored M protein with an in-frame deletion of the AB repeat region. Measurements of SpeB activity by cleavage of a substrate n-benzoyl-Pro-Phe-Arg-p-nitroanilide hydrochloride showed that the proteolytic activities in culture supernatants of both mutants were similar to those from the wild-type strain. In addition, Western blot analysis of culture supernatants showed that SpeB expression and processing to a mature form was unaffected by either deletion mutation. Therefore, we conclude that M protein is not required for maturation of the streptococcal cysteine protease SpeB." @default.
- W2105269145 created "2016-06-24" @default.
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- W2105269145 date "2005-02-01" @default.
- W2105269145 modified "2023-10-14" @default.
- W2105269145 title "The M Protein Is Dispensable for Maturation of Streptococcal Cysteine Protease SpeB" @default.
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- W2105269145 doi "https://doi.org/10.1128/iai.73.2.859-864.2005" @default.
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