Literature DB >> 14515151

Defense against own arms: staphylococcal cysteine proteases and their inhibitors.

Grzegorz Dubin1.   

Abstract

Staphylococcus aureus is a human pathogen causing a wide range of diseases. Most staphylococcal infections, unlike those caused by other bacteria are not toxigenic and very little is known about their pathogenesis. It has been proposed that a core of secreted proteins common to many infectious strains is responsible for colonization and infection. Among those proteins several proteases are present and over the years many different functions in the infection process have been attributed to them. However, little direct, in vivo data has been presented. Two cysteine proteases, staphopain A (ScpA) and staphopain B (SspB) are important members of this group of enzymes. Recently, two cysteine protease inhibitors, staphostatin A and staphostatin B (ScpB and SspC, respectively) were described in S. aureus shedding new light on the complexity of the processes involving the two proteases. The scope of this review is to summarize current knowledge on the network of staphylococcal cysteine proteases and their inhibitors in view of their possible role as virulence factors.

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Year:  2003        PMID: 14515151     DOI: 035003715

Source DB:  PubMed          Journal:  Acta Biochim Pol        ISSN: 0001-527X            Impact factor:   2.149


  4 in total

1.  Cytoplasmic control of premature activation of a secreted protease zymogen: deletion of staphostatin B (SspC) in Staphylococcus aureus 8325-4 yields a profound pleiotropic phenotype.

Authors:  Lindsey N Shaw; Ewa Golonka; Grzegorz Szmyd; Simon J Foster; James Travis; Jan Potempa
Journal:  J Bacteriol       Date:  2005-03       Impact factor: 3.490

2.  Superoxide dismutase, protease and lipase expression in clinical isolates of Staphylococcus aureus: a tool for antimicrobial drug discovery.

Authors:  Sanjai Saxena; Charu Gomber
Journal:  Mol Cell Biochem       Date:  2010-04-04       Impact factor: 3.396

3.  Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG.

Authors:  Katja Wenig; Lorenz Chatwell; Ulrich von Pawel-Rammingen; Lars Björck; Robert Huber; Peter Sondermann
Journal:  Proc Natl Acad Sci U S A       Date:  2004-12-01       Impact factor: 11.205

Review 4.  Regulation of bacterial protease activity.

Authors:  Benedykt Władyka; Katarzyna Pustelny
Journal:  Cell Mol Biol Lett       Date:  2008-04-10       Impact factor: 5.787

  4 in total

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