ArticleInfection and immunity2005
The M protein is dispensable for maturation of streptococcal cysteine protease SpeB.
Article in Infection and immunity, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- RNA-binding protein YebC enhances translation of proline-rich amino acid stretches in bacteria.Nature communications · 2025Article
- Repression of Rgg But Not Upregulation of LacD.1 inFrontiers in microbiology · 2016Article
- LL-37 Triggers Formation of Streptococcus pyogenes Extracellular Vesicle-Like Structures with Immune Stimulatory Properties.Journal of innate immunity · 2016Article
- Streptococcus pyogenes triggers activation of the human contact system by streptokinase.Infection and immunity · 2015Article
- The M1 protein of Streptococcus pyogenes triggers an innate uptake mechanism into polarized human endothelial cells.Journal of innate immunity · 2014Article
- A natural inactivating mutation in the CovS component of the CovRS regulatory operon in a pattern D Streptococcal pyogenes strain influences virulence-associated genes.The Journal of biological chemistry · 2013Article
- Protein F1 and Streptococcus pyogenes resistance to phagocytosis.Infection and immunity · 2007Article
- Role of streptococcal T antigens in superficial skin infection.Journal of bacteriology · 2007Article
- Identification and characterization of bicistronic speB and prsA gene expression in the group A Streptococcus.Journal of bacteriology · 2006Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.