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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2254561
- author
- Nelson, Daniel C.
; Garbe, Julia
LU
and Collin, Mattias
LU
- organization
- publishing date
- 2011
- 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
- 10.1515/BC.2011.208
- language
- English
- LU publication?
- yes
- id
- 2619c869-bca5-4a03-8164-8aa9c5b25231 (old id 2254561)
- date added to LUP
- 2016-04-01 10:52:40
- date last changed
- 2022-04-28 02:18:55
@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}},
keywords = {{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/10.1515/BC.2011.208}},
doi = {{10.1515/BC.2011.208}},
volume = {{392}},
year = {{2011}},
}