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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1123214
- author
- Collin, Mattias
LU
and Olsén, Arne
LU
- organization
- publishing date
- 2001
- 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
- 2016-04-01 16:50:11
- date last changed
- 2022-04-23 00:49:41
@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}},
keywords = {{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}},
doi = {{10.1093/emboj/20.12.3046}},
volume = {{20}},
year = {{2001}},
}