The M protein is dispensable for maturation of streptococcal cysteine protease SpeB

Björn Zimmerlein, Hae Sun Park, Shaoying Li, Andreas Podbielski, P. Patrick Cleary

Research output: Contribution to journalArticlepeer-review

11 Scopus citations


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. Olsén, Mol. Microbiol. 36:1306-1318, 2000). Collin and Olsén 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.

Original languageEnglish (US)
Pages (from-to)859-864
Number of pages6
JournalInfection and Immunity
Issue number2
StatePublished - Feb 2005
Externally publishedYes

ASJC Scopus subject areas

  • Parasitology
  • Microbiology
  • Immunology
  • Infectious Diseases


Dive into the research topics of 'The M protein is dispensable for maturation of streptococcal cysteine protease SpeB'. Together they form a unique fingerprint.

Cite this