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- W2012365327 endingPage "1088" @default.
- W2012365327 startingPage "1077" @default.
- W2012365327 abstract "Group A streptococcus (Streptococcus pyogenes) is an exclusively human pathogen that causes a wide spectrum of diseases ranging from pharyngitis, to impetigo, to toxic shock, to necrotizing fasciitis. The diversity of these disease states necessitates that S. pyogenes possess the ability to modulate both the innate and adaptive immune responses. SpeB, a cysteine proteinase, is the predominant secreted protein from S. pyogenes. Because of its relatively indiscriminant specificity, this enzyme has been shown to degrade the extracellular matrix, cytokines, chemokines, complement components, immunoglobulins, and serum protease inhibitors, to name but a few of the known substrates. Additionally, SpeB regulates other streptococcal proteins by degrading them or releasing them from the bacterial surface. Despite the wealth of literature on putative SpeB functions, there remains much controversy about this enzyme because many of reported activities would produce contradictory physiological results. Here we review all known host and bacterial protein substrates for SpeB, their cleavage sites, and discuss the role of this enzyme in streptococcal pathogenesis based on the current literature." @default.
- W2012365327 created "2016-06-24" @default.
- W2012365327 creator A5002941041 @default.
- W2012365327 creator A5075146072 @default.
- W2012365327 creator A5087338698 @default.
- W2012365327 date "2011-12-01" @default.
- W2012365327 modified "2023-10-13" @default.
- W2012365327 title "Cysteine proteinase SpeB from <i>Streptococcus pyogenes</i> – a potent modifier of immunologically important host and bacterial proteins" @default.
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