Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules

Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules

Autotransporter proteins are localised to the bacterial surface and promote colonisation of host epithelial surfaces. Here, the authors present the crystal structure of autotransporter UpaB and show evidence for distinct binding sites for glycosaminoglycans and host fibronectin.

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Autores principales: Jason J. Paxman, Alvin W. Lo, Matthew J. Sullivan, Santosh Panjikar, Michael Kuiper, Andrew E. Whitten, Geqing Wang, Chi-Hao Luan, Danilo G. Moriel, Lendl Tan, Kate M. Peters, Minh-Duy Phan, Christine L. Gee, Glen C. Ulett, Mark A. Schembri, Begoña Heras
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/84181b0a975c40f082db3fb0320d1436
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spelling oai:doaj.org-article:84181b0a975c40f082db3fb0320d14362021-12-02T14:39:19ZUnique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules10.1038/s41467-019-09814-62041-1723https://doaj.org/article/84181b0a975c40f082db3fb0320d14362019-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-09814-6https://doaj.org/toc/2041-1723Autotransporter proteins are localised to the bacterial surface and promote colonisation of host epithelial surfaces. Here, the authors present the crystal structure of autotransporter UpaB and show evidence for distinct binding sites for glycosaminoglycans and host fibronectin.Jason J. PaxmanAlvin W. LoMatthew J. SullivanSantosh PanjikarMichael KuiperAndrew E. WhittenGeqing WangChi-Hao LuanDanilo G. MorielLendl TanKate M. PetersMinh-Duy PhanChristine L. GeeGlen C. UlettMark A. SchembriBegoña HerasNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Jason J. Paxman
Alvin W. Lo
Matthew J. Sullivan
Santosh Panjikar
Michael Kuiper
Andrew E. Whitten
Geqing Wang
Chi-Hao Luan
Danilo G. Moriel
Lendl Tan
Kate M. Peters
Minh-Duy Phan
Christine L. Gee
Glen C. Ulett
Mark A. Schembri
Begoña Heras
Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules
description Autotransporter proteins are localised to the bacterial surface and promote colonisation of host epithelial surfaces. Here, the authors present the crystal structure of autotransporter UpaB and show evidence for distinct binding sites for glycosaminoglycans and host fibronectin.
format article
author Jason J. Paxman
Alvin W. Lo
Matthew J. Sullivan
Santosh Panjikar
Michael Kuiper
Andrew E. Whitten
Geqing Wang
Chi-Hao Luan
Danilo G. Moriel
Lendl Tan
Kate M. Peters
Minh-Duy Phan
Christine L. Gee
Glen C. Ulett
Mark A. Schembri
Begoña Heras
author_facet Jason J. Paxman
Alvin W. Lo
Matthew J. Sullivan
Santosh Panjikar
Michael Kuiper
Andrew E. Whitten
Geqing Wang
Chi-Hao Luan
Danilo G. Moriel
Lendl Tan
Kate M. Peters
Minh-Duy Phan
Christine L. Gee
Glen C. Ulett
Mark A. Schembri
Begoña Heras
author_sort Jason J. Paxman
title Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules
title_short Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules
title_full Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules
title_fullStr Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules
title_full_unstemmed Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules
title_sort unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/84181b0a975c40f082db3fb0320d1436
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