Intimin and invasin export their C-terminus to the bacterial cell surface using an inverse mechanism compared to classical autotransport.

Invasin and intimin are major virulence factors of enteropathogenic Yersiniae and Escherichia coli, mediating invasion into and intimate adherence to host cells, respectively. Several studies have hinted that extracellular portion of these homologous proteins might be exported via an autotransport m...

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Autores principales:	Philipp Oberhettinger, Monika Schütz, Jack C Leo, Nadja Heinz, Jürgen Berger, Ingo B Autenrieth, Dirk Linke
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/dc0d1063fb5645a6b87fe609b9247f85
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spelling	oai:doaj.org-article:dc0d1063fb5645a6b87fe609b9247f852021-11-18T08:12:41ZIntimin and invasin export their C-terminus to the bacterial cell surface using an inverse mechanism compared to classical autotransport.1932-620310.1371/journal.pone.0047069https://doaj.org/article/dc0d1063fb5645a6b87fe609b9247f852012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23056583/?tool=EBIhttps://doaj.org/toc/1932-6203Invasin and intimin are major virulence factors of enteropathogenic Yersiniae and Escherichia coli, mediating invasion into and intimate adherence to host cells, respectively. Several studies have hinted that extracellular portion of these homologous proteins might be exported via an autotransport mechanism, but rigorous experimental proof has been lacking. Here, we present a topology model for invasin and intimin, consistent with the hypothesis that the N-terminal β-barrel domain acts as a translocation pore to secrete the C-terminal passenger domain. We confirmed this topology model by inserting epitope tags into the loops of the β-barrel. We further show that obstructing the pore of β-barrel hinders the export of the passenger domain. As for classical autotransport, the biogenesis of invasin and intimin is dependent on the Bam complex and the periplasmic chaperone SurA, whereas the chaperone/protease DegP is involved in quality control. However, compared to classical autotransporters (Type Va secretion), the domain structure of intimin and invasin is inverted. We conclude that proteins of the intimin and invasin family constitute a novel group of autotransported proteins, and propose that this class of autotransporters be termed Type Ve secretion.Philipp OberhettingerMonika SchützJack C LeoNadja HeinzJürgen BergerIngo B AutenriethDirk LinkePublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 10, p e47069 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Philipp Oberhettinger Monika Schütz Jack C Leo Nadja Heinz Jürgen Berger Ingo B Autenrieth Dirk Linke Intimin and invasin export their C-terminus to the bacterial cell surface using an inverse mechanism compared to classical autotransport.
description	Invasin and intimin are major virulence factors of enteropathogenic Yersiniae and Escherichia coli, mediating invasion into and intimate adherence to host cells, respectively. Several studies have hinted that extracellular portion of these homologous proteins might be exported via an autotransport mechanism, but rigorous experimental proof has been lacking. Here, we present a topology model for invasin and intimin, consistent with the hypothesis that the N-terminal β-barrel domain acts as a translocation pore to secrete the C-terminal passenger domain. We confirmed this topology model by inserting epitope tags into the loops of the β-barrel. We further show that obstructing the pore of β-barrel hinders the export of the passenger domain. As for classical autotransport, the biogenesis of invasin and intimin is dependent on the Bam complex and the periplasmic chaperone SurA, whereas the chaperone/protease DegP is involved in quality control. However, compared to classical autotransporters (Type Va secretion), the domain structure of intimin and invasin is inverted. We conclude that proteins of the intimin and invasin family constitute a novel group of autotransported proteins, and propose that this class of autotransporters be termed Type Ve secretion.
format	article
author	Philipp Oberhettinger Monika Schütz Jack C Leo Nadja Heinz Jürgen Berger Ingo B Autenrieth Dirk Linke
author_facet	Philipp Oberhettinger Monika Schütz Jack C Leo Nadja Heinz Jürgen Berger Ingo B Autenrieth Dirk Linke
author_sort	Philipp Oberhettinger
title	Intimin and invasin export their C-terminus to the bacterial cell surface using an inverse mechanism compared to classical autotransport.
title_short	Intimin and invasin export their C-terminus to the bacterial cell surface using an inverse mechanism compared to classical autotransport.
title_full	Intimin and invasin export their C-terminus to the bacterial cell surface using an inverse mechanism compared to classical autotransport.
title_fullStr	Intimin and invasin export their C-terminus to the bacterial cell surface using an inverse mechanism compared to classical autotransport.
title_full_unstemmed	Intimin and invasin export their C-terminus to the bacterial cell surface using an inverse mechanism compared to classical autotransport.
title_sort	intimin and invasin export their c-terminus to the bacterial cell surface using an inverse mechanism compared to classical autotransport.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/dc0d1063fb5645a6b87fe609b9247f85
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Intimin and invasin export their C-terminus to the bacterial cell surface using an inverse mechanism compared to classical autotransport.

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