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EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG

Collin, Mattias LU and Olsén, Arne LU (2001) In EMBO Journal 20(12). p.3046-3055
Abstract
Streptococcus pyogenes is an important human pathogen that selectively interacts with proteins involved in the humoral defense system, such as immunoglobulins and complement factors. In this report we show that S.pyogenes has the ability to hydrolyze the chitobiose core of the asparagine-linked glycan on immuno globulin G (IgG) when bacteria are grown in the presence of human plasma. This activity is associated with the secretion of a novel 108 kDa protein denoted EndoS. EndoS has endoglycosidase activity on purified soluble IgG as well as IgG bound to the bacterial surface. EndoS is required for the activity on IgG, as an isogenic EndoS mutant could not hydrolyze the glycan on IgG. In addition, we show that the secreted streptococcal... (More)
Streptococcus pyogenes is an important human pathogen that selectively interacts with proteins involved in the humoral defense system, such as immunoglobulins and complement factors. In this report we show that S.pyogenes has the ability to hydrolyze the chitobiose core of the asparagine-linked glycan on immuno globulin G (IgG) when bacteria are grown in the presence of human plasma. This activity is associated with the secretion of a novel 108 kDa protein denoted EndoS. EndoS has endoglycosidase activity on purified soluble IgG as well as IgG bound to the bacterial surface. EndoS is required for the activity on IgG, as an isogenic EndoS mutant could not hydrolyze the glycan on IgG. In addition, we show that the secreted streptococcal cysteine proteinase SpeB cleaves IgG in the hinge region in a papain-like manner. This is the first example of an endoglycosidase produced by a bacterial pathogen that selectively hydrolyzes human IgG, and reveals a novel mechanism which may contribute to S.pyogenes pathogenesis. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
cysteine proteinase, endo-beta-N-acetylglucos aminidase, endoglycosidase, IgG, Streptococcus pyogenes
in
EMBO Journal
volume
20
issue
12
pages
3046 - 3055
publisher
Oxford University Press
external identifiers
  • pmid:11406581
  • scopus:0035875889
ISSN
1460-2075
DOI
10.1093/emboj/20.12.3046
language
English
LU publication?
yes
id
9e3c5514-e04b-4819-9991-839825931899 (old id 1123214)
alternative location
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC150189/
date added to LUP
2008-06-26 09:14:34
date last changed
2018-08-05 04:13:15
@article{9e3c5514-e04b-4819-9991-839825931899,
  abstract     = {Streptococcus pyogenes is an important human pathogen that selectively interacts with proteins involved in the humoral defense system, such as immunoglobulins and complement factors. In this report we show that S.pyogenes has the ability to hydrolyze the chitobiose core of the asparagine-linked glycan on immuno globulin G (IgG) when bacteria are grown in the presence of human plasma. This activity is associated with the secretion of a novel 108 kDa protein denoted EndoS. EndoS has endoglycosidase activity on purified soluble IgG as well as IgG bound to the bacterial surface. EndoS is required for the activity on IgG, as an isogenic EndoS mutant could not hydrolyze the glycan on IgG. In addition, we show that the secreted streptococcal cysteine proteinase SpeB cleaves IgG in the hinge region in a papain-like manner. This is the first example of an endoglycosidase produced by a bacterial pathogen that selectively hydrolyzes human IgG, and reveals a novel mechanism which may contribute to S.pyogenes pathogenesis.},
  author       = {Collin, Mattias and Olsén, Arne},
  issn         = {1460-2075},
  keyword      = {cysteine proteinase,endo-beta-N-acetylglucos aminidase,endoglycosidase,IgG,Streptococcus pyogenes},
  language     = {eng},
  number       = {12},
  pages        = {3046--3055},
  publisher    = {Oxford University Press},
  series       = {EMBO Journal},
  title        = {EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG},
  url          = {http://dx.doi.org/10.1093/emboj/20.12.3046},
  volume       = {20},
  year         = {2001},
}