Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Help & Advice
University of Warwick

The Library

  • Login
  • Admin

Fragments of bacterial endoglycosidase S and immunoglobulin G reveal subdomains of each that contribute to deglycosylation

Tools
- Tools
+ Tools

Dixon, Emma V., Claridge, Jolyon K., Harvey, David J., Baruah, Kavitha, Yu, Xiaojie, Vesiljevic, Snezana, Mattick, Susan, Pritchard, Laura K., Krishna, Benjamin, Scanlan, Christopher N., Schnell, Jason R., Higgins, Matthew K., Zitzmann, Nicole and Crispin, Max (2014) Fragments of bacterial endoglycosidase S and immunoglobulin G reveal subdomains of each that contribute to deglycosylation. Journal of Biological Chemistry, Volume 289 (Number 20). pp. 13876-13889. doi:10.1074/jbc.M113.532812 ISSN 0021-9258.

[img]
Preview
PDF
WRAP_13876.full.pdf - Published Version - Requires a PDF viewer.
Available under License Creative Commons Attribution.

Download (3591Kb) | Preview
Official URL: http://dx.doi.org/10.1074/jbc.M113.532812

Request Changes to record.

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 isolated CH2 domain of the Fc domain. Similarly, we sought to investigate which domains within EndoS could contribute to activity. Bioinformatics analysis of the domain organization of EndoS confirmed the previous predictions of a chitinase domain and leucine-rich repeat but also revealed a putative carbohydrate binding module (CBM) followed by a C-terminal region. Using expressed fragments of EndoS, circular dichroism of the isolated CBM, and a CBM-C-terminal region fusion revealed folded domains dominated by β sheet and α helical structure, respectively. Nuclear magnetic resonance analysis of the CBM with monosaccharides was suggestive of carbohydrate binding functionality. Functional analysis of truncations of EndoS revealed that, whereas the C-terminal of EndoS is dispensable for activity, its deletion impedes the hydrolysis of IgG glycans.

Item Type: Journal Article
Subjects: Q Science > QR Microbiology
Divisions: Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
Library of Congress Subject Headings (LCSH): Endoglycosidases, Streptococcus pyogenes
Journal or Publication Title: Journal of Biological Chemistry
Publisher: American Society for Biochemistry and Molecular Biology
ISSN: 0021-9258
Official Date: 16 May 2014
Dates:
DateEvent
16 May 2014Published
25 March 2014Available
Volume: Volume 289
Number: Number 20
Page Range: pp. 13876-13889
DOI: 10.1074/jbc.M113.532812
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access (Creative Commons)
Date of first compliant deposit: 28 December 2015
Date of first compliant Open Access: 28 December 2015
Funder: Medical Research Council (Great Britain) (MRC), University of Oxford. Oxford Glycobiology Institute, Wellcome Trust (London, England), Clarendon Fund (CF), Universities New Zealand (Organization), Seventh Framework Programme (European Commission) (FP7)
Grant number: 261863 (FP7)

Request changes or add full text files to a record

Repository staff actions (login required)

View Item View Item

Downloads

Downloads per month over past year

View more statistics

twitter

Email us: wrap@warwick.ac.uk
Contact Details
About Us