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Cysteine proteinase SpeB from Streptococcus pyogenes - a potent modifier of immunologically important host and bacterial proteins

Nelson, Daniel C.; Garbe, Julia LU and Collin, Mattias LU (2011) In Biological Chemistry 392(12). p.1077-1088
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
animal models, C10 cysteine proteinase, human infection, immune, evasion, proteolysis, SpeB, streptococcal cysteine proteinase, streptopain, virulence
in
Biological Chemistry
volume
392
issue
12
pages
1077 - 1088
publisher
De Gruyter
external identifiers
  • wos:000296773000002
  • scopus:80755169615
ISSN
1437-4315
DOI
https://doi.org/10.1515/BC.2011.208
language
English
LU publication?
yes
id
2619c869-bca5-4a03-8164-8aa9c5b25231 (old id 2254561)
date added to LUP
2012-01-02 08:10:04
date last changed
2017-11-14 09:51:59
@article{2619c869-bca5-4a03-8164-8aa9c5b25231,
  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.},
  author       = {Nelson, Daniel C. and Garbe, Julia and Collin, Mattias},
  issn         = {1437-4315},
  keyword      = {animal models,C10 cysteine proteinase,human infection,immune,evasion,proteolysis,SpeB,streptococcal cysteine proteinase,streptopain,virulence},
  language     = {eng},
  number       = {12},
  pages        = {1077--1088},
  publisher    = {De Gruyter},
  series       = {Biological Chemistry},
  title        = {Cysteine proteinase SpeB from Streptococcus pyogenes - a potent modifier of immunologically important host and bacterial proteins},
  url          = {http://dx.doi.org/https://doi.org/10.1515/BC.2011.208},
  volume       = {392},
  year         = {2011},
}