EndoS2 is a unique and conserved enzyme of serotype M49 group A Streptococcus that hydrolyses N-linked glycans on IgG and α1-acid glycoprotein
Sjögren, Jonathan LU ; Struwe, Weston B. ; Cosgrave, Eoin F. J. ; Rudd, Pauline M. ; Stervander, Martin LU ; Allhorn, Maria LU ; Hollands, Andrew ; Nizet, Victor and Collin, Mattias LU
(2013)
In Biochemical Journal
455(1).
p.107-118
- Abstract
- Many bacteria have evolved ways to interact with glycosylation functions of the immune system of their hosts. Streptococcus pyogenes [GAS (group A Streptococcus)] secretes the enzyme EndoS that cleaves glycans on human IgG and impairs the effector functions of the antibody. The ndoS gene, encoding EndoS, has, until now, been thought to be conserved throughout the serotypes. However, in the present study, we identify EndoS2, an endoglycosidase in serotype M49 GAS strains. We characterized EndoS2 and the corresponding ndoS2 gene using sequencing, bioinformatics, phylogenetic analysis, recombinant expression and LC–MS analysis of glycosidic activity. This revealed that EndoS2 is present exclusively, and highly conserved, in serotype M49 of... (More)
- Many bacteria have evolved ways to interact with glycosylation functions of the immune system of their hosts. Streptococcus pyogenes [GAS (group A Streptococcus)] secretes the enzyme EndoS that cleaves glycans on human IgG and impairs the effector functions of the antibody. The ndoS gene, encoding EndoS, has, until now, been thought to be conserved throughout the serotypes. However, in the present study, we identify EndoS2, an endoglycosidase in serotype M49 GAS strains. We characterized EndoS2 and the corresponding ndoS2 gene using sequencing, bioinformatics, phylogenetic analysis, recombinant expression and LC–MS analysis of glycosidic activity. This revealed that EndoS2 is present exclusively, and highly conserved, in serotype M49 of GAS and is only 37% identical with EndoS. EndoS2 showed endo-β-N-acetylglucosaminidase activity on all N-linked glycans of IgG and on biantennary and sialylated glycans of AGP (α1-acid glycoprotein). The enzyme was found to act only on native IgG and AGP and to be specific for free biantennary glycans with or without terminal sialylation. GAS M49 expression of EndoS2 was monitored in relation to carbohydrates present in the culture medium and was linked to the presence of sucrose. We conclude that EndoS2 is a unique endoglycosidase in serotype M49 and differs from EndoS of other GAS strains by targeting both IgG and AGP. EndoS2 expands the repertoire of GAS effectors that modify key glycosylated molecules of host defence. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4146763
- author
- Sjögren, Jonathan
LU
; Struwe, Weston B.
; Cosgrave, Eoin F. J.
; Rudd, Pauline M.
; Stervander, Martin
LU
; Allhorn, Maria
LU
; Hollands, Andrew
; Nizet, Victor
and Collin, Mattias
LU
- organization
- publishing date
- 2013
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- endo-β-N-acetylglucosaminidase, host–pathogen interaction, α1-acid glycoprotein, IgG glycosylation, Streptococcus pyogenes
- in
- Biochemical Journal
- volume
- 455
- issue
- 1
- pages
- 107 - 118
- publisher
- Portland Press
- external identifiers
-
- wos:000329843200011
- scopus:84884230691
- ISSN
- 0264-6021
- DOI
- 10.1042/BJ20130126
- language
- English
- LU publication?
- yes
- id
- 6a73c5df-ba16-479e-ab03-1037df2fd072 (old id 4146763)
- alternative location
- http://www.biochemj.org/bj/455/0107/4550107.pdf
- date added to LUP
- 2016-04-01 10:04:09
- date last changed
- 2024-05-06 02:17:33
@article{6a73c5df-ba16-479e-ab03-1037df2fd072,
abstract = {{Many bacteria have evolved ways to interact with glycosylation functions of the immune system of their hosts. Streptococcus pyogenes [GAS (group A Streptococcus)] secretes the enzyme EndoS that cleaves glycans on human IgG and impairs the effector functions of the antibody. The ndoS gene, encoding EndoS, has, until now, been thought to be conserved throughout the serotypes. However, in the present study, we identify EndoS2, an endoglycosidase in serotype M49 GAS strains. We characterized EndoS2 and the corresponding ndoS2 gene using sequencing, bioinformatics, phylogenetic analysis, recombinant expression and LC–MS analysis of glycosidic activity. This revealed that EndoS2 is present exclusively, and highly conserved, in serotype M49 of GAS and is only 37% identical with EndoS. EndoS2 showed endo-β-N-acetylglucosaminidase activity on all N-linked glycans of IgG and on biantennary and sialylated glycans of AGP (α1-acid glycoprotein). The enzyme was found to act only on native IgG and AGP and to be specific for free biantennary glycans with or without terminal sialylation. GAS M49 expression of EndoS2 was monitored in relation to carbohydrates present in the culture medium and was linked to the presence of sucrose. We conclude that EndoS2 is a unique endoglycosidase in serotype M49 and differs from EndoS of other GAS strains by targeting both IgG and AGP. EndoS2 expands the repertoire of GAS effectors that modify key glycosylated molecules of host defence.}},
author = {{Sjögren, Jonathan and Struwe, Weston B. and Cosgrave, Eoin F. J. and Rudd, Pauline M. and Stervander, Martin and Allhorn, Maria and Hollands, Andrew and Nizet, Victor and Collin, Mattias}},
issn = {{0264-6021}},
keywords = {{endo-β-N-acetylglucosaminidase; host–pathogen interaction; α1-acid glycoprotein; IgG glycosylation; Streptococcus pyogenes}},
language = {{eng}},
number = {{1}},
pages = {{107--118}},
publisher = {{Portland Press}},
series = {{Biochemical Journal}},
title = {{EndoS2 is a unique and conserved enzyme of serotype M49 group A Streptococcus that hydrolyses N-linked glycans on IgG and α1-acid glycoprotein}},
url = {{http://dx.doi.org/10.1042/BJ20130126}},
doi = {{10.1042/BJ20130126}},
volume = {{455}},
year = {{2013}},
}