dc.contributor.author |
Linke, Christian |
en |
dc.contributor.author |
Caradoc-Davies, Thomas |
en |
dc.contributor.author |
Young, Paul |
en |
dc.contributor.author |
Proft, Thomas |
en |
dc.contributor.author |
Baker, Edward |
en |
dc.date.accessioned |
2012-02-23T00:23:36Z |
en |
dc.date.issued |
2009 |
en |
dc.identifier.citation |
J BACTERIOL 191(18):5814-5823 15 Sep 2009 |
en |
dc.identifier.issn |
0021-9193 |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/11687 |
en |
dc.description.abstract |
The common pathogen Streptococcus pyogenes colonizes the human skin and tonsils and can invade underlying tissues. This requires the adhesion of S. pyogenes to host surface receptors mediated through adhesins. The laminin-binding protein Lbp has been suggested as an adhesin, specific for the human extracellular matrix protein laminin. Sequence alignments, however, indicate a relationship between Lbp and a family of bacterial metal-binding receptors. To further analyze the role of Lbp in S. pyogenes and its potential role in pathogenicity, Lbp has been crystallized, and its structure has been solved at a resolution of 2.45 Å (R = 0.186; Rfree = 0.251). Lbp has the typical metal-binding receptor fold, comprising two globular (²/)4 domains connected by a helical backbone. The two domains enclose the metal-binding site, which contains a zinc ion. The interaction of Lbp with laminin was further investigated and shown to be specific in vitro. Localization studies with antibodies specific for Lbp show that the protein is attached to the membrane. The data suggest that Lbp is primarily a zinc-binding protein, and we suggest that its interaction with laminin in vivo may be mediated via zinc bound to laminin. |
en |
dc.description.uri |
http://jb.asm.org/cgi/content/full/191/18/5814?view=long&pmid=19617361 |
en |
dc.publisher |
American Society for Microbiology |
en |
dc.relation.ispartofseries |
Journal of Bacteriology |
en |
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher.
Details obtained from http://www.sherpa.ac.uk/romeo/issn/0021-9193/ |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
en |
dc.title |
The laminin-binding protein Lbp from Streptococcus pyogenes is a zinc receptor |
en |
dc.type |
Journal Article |
en |
dc.identifier.doi |
10.1128/JB.00485-09 |
en |
pubs.issue |
18 |
en |
pubs.begin-page |
5814 |
en |
pubs.volume |
191 |
en |
dc.rights.holder |
Copyright: American Society for Microbiology |
en |
dc.identifier.pmid |
19617361 |
en |
pubs.end-page |
5823 |
en |
dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Article |
en |
pubs.elements-id |
86550 |
en |
pubs.org-id |
Medical and Health Sciences |
en |
pubs.org-id |
Medical Sciences |
en |
pubs.org-id |
Molecular Medicine |
en |
pubs.org-id |
Science |
en |
pubs.org-id |
Biological Sciences |
en |
pubs.org-id |
Science Research |
en |
pubs.org-id |
Maurice Wilkins Centre (2010-2014) |
en |
pubs.record-created-at-source-date |
2010-09-01 |
en |
pubs.dimensions-id |
19617361 |
en |