Structural details of human tuba recruitment by InlC of Listeria monocytogenes elucidate bacterial cell-cell spreading

Structure
Lilia PolleWolf-Dieter Schubert

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.

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Citations

Jun 21, 2014·Cellular Microbiology·Keith IretonGeorgina C Dowd
May 30, 2015·Trends in Microbiology·Carole J KuehlHervé Agaisse
Jun 10, 2015·Acta Crystallographica. Section D, Biological Crystallography·Isabelle MirasMathieu Picardeau
Nov 11, 2016·Cell Host & Microbe·Keith Ireton
Feb 6, 2020·Proceedings of the National Academy of Sciences of the United States of America·Georgina C DowdKeith Ireton
Jul 20, 2020·Trends in Microbiology·Georgina C DowdKeith Ireton
Dec 14, 2018·Microbiology Spectrum·Javier Pizarro-Cerdá, Pascale Cossart
Oct 6, 2021·Molecular Microbiology·Thilina U B HerathKeith Ireton
Oct 28, 2021·Molecular Microbiology·Keith IretonMazhar Hussain

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