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Study of the IgG endoglycosidase EndoS in group A streptococcal phagocyte resistance and virulence

Sjögren, Jonathan LU ; Okumura, Cheryl Y. M.; Collin, Mattias LU ; Nizet, Victor and Hollands, Andrew (2011) In BMC Microbiology 11.
Abstract
Background: The secreted enzyme EndoS, an endoglycosidase from Streptococcus pyogenes, hydrolyzes the N-linked glycan of the constant region of immunoglobulin G (IgG) heavy chain and renders the antibody unable to interact with Fc receptors and elicit effector functions. In this study we couple targeted allelic replacement mutagenesis and heterologous expression to elucidate the contribution of EndoS to group A Streptococcus (GAS) phagocyte resistance and pathogenicity in vitro and in vivo. Results: Knocking out the EndoS gene in GAS M1T1 background revealed no significant differences in bacterial survival in immune cell killing assays or in a systemic mouse model of infection. However, exogenous addition and heterologous expression of... (More)
Background: The secreted enzyme EndoS, an endoglycosidase from Streptococcus pyogenes, hydrolyzes the N-linked glycan of the constant region of immunoglobulin G (IgG) heavy chain and renders the antibody unable to interact with Fc receptors and elicit effector functions. In this study we couple targeted allelic replacement mutagenesis and heterologous expression to elucidate the contribution of EndoS to group A Streptococcus (GAS) phagocyte resistance and pathogenicity in vitro and in vivo. Results: Knocking out the EndoS gene in GAS M1T1 background revealed no significant differences in bacterial survival in immune cell killing assays or in a systemic mouse model of infection. However, exogenous addition and heterologous expression of EndoS was found to increase GAS resistance to killing by neutrophils and monocytes in vitro. Additionally, heterologous expression of EndoS in M49 GAS increased mouse virulence in vivo. Conclusions: We conclude that in a highly virulent M1T1 background, EndoS has no significant impact on GAS phagocyte resistance and pathogenicity. However, local accumulation or high levels of expression of EndoS in certain GAS strains may contribute to virulence. (Less)
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organization
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type
Contribution to journal
publication status
published
subject
in
BMC Microbiology
volume
11
publisher
BioMed Central
external identifiers
  • wos:000292155700001
  • scopus:79957456998
ISSN
1471-2180
DOI
10.1186/1471-2180-11-120
language
English
LU publication?
yes
id
1cff886c-6c6d-46c0-a04f-6d8bd5971559 (old id 2049229)
date added to LUP
2011-08-02 08:59:21
date last changed
2017-07-30 04:21:37
@article{1cff886c-6c6d-46c0-a04f-6d8bd5971559,
  abstract     = {Background: The secreted enzyme EndoS, an endoglycosidase from Streptococcus pyogenes, hydrolyzes the N-linked glycan of the constant region of immunoglobulin G (IgG) heavy chain and renders the antibody unable to interact with Fc receptors and elicit effector functions. In this study we couple targeted allelic replacement mutagenesis and heterologous expression to elucidate the contribution of EndoS to group A Streptococcus (GAS) phagocyte resistance and pathogenicity in vitro and in vivo. Results: Knocking out the EndoS gene in GAS M1T1 background revealed no significant differences in bacterial survival in immune cell killing assays or in a systemic mouse model of infection. However, exogenous addition and heterologous expression of EndoS was found to increase GAS resistance to killing by neutrophils and monocytes in vitro. Additionally, heterologous expression of EndoS in M49 GAS increased mouse virulence in vivo. Conclusions: We conclude that in a highly virulent M1T1 background, EndoS has no significant impact on GAS phagocyte resistance and pathogenicity. However, local accumulation or high levels of expression of EndoS in certain GAS strains may contribute to virulence.},
  author       = {Sjögren, Jonathan and Okumura, Cheryl Y. M. and Collin, Mattias and Nizet, Victor and Hollands, Andrew},
  issn         = {1471-2180},
  language     = {eng},
  publisher    = {BioMed Central},
  series       = {BMC Microbiology},
  title        = {Study of the IgG endoglycosidase EndoS in group A streptococcal phagocyte resistance and virulence},
  url          = {http://dx.doi.org/10.1186/1471-2180-11-120},
  volume       = {11},
  year         = {2011},
}