dc.contributor.author |
Polle, Lilia
|
|
dc.contributor.author |
Rigano, Luciano
|
|
dc.contributor.author |
Julian, Rowan
|
|
dc.contributor.author |
Ireton, Keith
|
|
dc.contributor.author |
Schubert, Wolf-Dieter
|
|
dc.date.accessioned |
2014-05-22T08:57:39Z |
|
dc.date.available |
2014-05-22T08:57:39Z |
|
dc.date.issued |
2014-02 |
|
dc.description.abstract |
The human pathogen Listeria monocytogenes is able to directly spread to neighboring cells of host tissues, a process recently linked to the virulence factor InlC. InlC targets the sixth SH3 domain (SH3-6) of human Tuba, disrupting its physiological interaction with the cytoskeletal protein N-WASP. The resulting loss of cortical actin tension may slacken the junctional membrane, allowing protrusion formation by motile Listeria. Complexes of Tuba SH3-6 with physiological partners N-WASP and Mena reveal equivalent binding modes but distinct affinities. The interaction surface of the infection complex InlC/Tuba SH3-6 is centered on phenylalanine 146 of InlC stacking upon asparagine 1569 of Tuba. Replacing Phe146 by alanine largely abrogates molecular affinity and in vivo mimics deletion of inlC. Collectively, our findings indicate that InlC hijacks Tuba through its LRR domain, blocking the peptide binding groove to prevent recruitment of its physiological partners. |
en_US |
dc.description.librarian |
hb2014 |
en_US |
dc.description.sponsorship |
Medical Research Council and the National Research Foundation of South Africa. National Institutes of Health (grant R01AI085072) |
en_US |
dc.description.uri |
http://www.journals.elsevier.com/structure |
en_US |
dc.identifier.citation |
Polle, L, Rigano, LA, Julian, R, Ireton, K & Schubert, WD 2014, 'Structural details of human tuba recruitment by InlC of Listeria monocytogenes elucidate bacterial cell-cell spreading', Structure, vol. 22, no. 2, pp. 304-314. |
en_US |
dc.identifier.issn |
0969-2126 (print) |
|
dc.identifier.issn |
1878-4186 (online) |
|
dc.identifier.other |
10.1016/j.str.2013.10.017 |
|
dc.identifier.uri |
http://hdl.handle.net/2263/39848 |
|
dc.language.iso |
en |
en_US |
dc.publisher |
Elsevier |
en_US |
dc.rights |
© 2014 Elsevier B.V. All rights reserved.Notice : this is the author’s version of a work that was accepted for publication in Structure. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Structure, vol. 22, no. 2, pp.304-314, 2014. doi : 10.1016/j.str.2013.10.017. |
en_US |
dc.subject |
Molecular mechanism of infection |
en_US |
dc.subject |
Engineering of protein-protein interactions |
en_US |
dc.subject |
LRR proteins |
en_US |
dc.title |
Structural details of human tuba recruitment by InlC of Listeria monocytogenes elucidate bacterial cell-cell spreading |
en_US |
dc.type |
Postprint Article |
en_US |