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Fragments of bacterial endoglycosidase s and immunoglobulin g reveal subdomains of each that contribute to deglycosylation.

Abstract:

Endoglycosidase S (EndoS) is a glycoside-hydrolase secreted by the bacterium Streptococcus pyogenes. EndoS preferentially hydrolyzes the N-linked glycans from the Fc region of IgG during infection. This hydrolysis impedes Fc functionality and contributes to the immune evasion strategy of S. pyogenes. Here, we investigate the mechanism of human serum IgG deactivation by EndoS. We expressed fragments of IgG1 and demonstrated that EndoS was catalytically active against all of them including the ...

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Publication status:
Published
Peer review status:
Peer reviewed

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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
More from this funder
Name:
European Commission’s Framework Program 7
More from this funder
Name:
William Georgetti Scholarship
More from this funder
Name:
Oxford Glycobiology Endowment
Publisher:
American Society for Biochemistry and Molecular Biology
Journal:
Journal of Biological Chemistry More from this journal
Volume:
289
Issue:
20
Pages:
13876-13889
Publication date:
2014-05-01
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Language:
English
Keywords:
Pubs id:
pubs:458653
UUID:
uuid:a92ccc57-4351-4f2d-af32-d7c1ab8a51eb
Local pid:
pubs:458653
Source identifiers:
458653
Deposit date:
2016-02-03

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