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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doaj-dc0d1063fb5645a6b87fe609b9247f852021-03-04T00:12:34ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-01710e4706910.1371/journal.pone.0047069Intimin and invasin export their C-terminus to the bacterial cell surface using an inverse mechanism compared to classical autotransport.Philipp OberhettingerMonika SchützJack C LeoNadja HeinzJürgen BergerIngo B AutenriethDirk LinkeInvasin 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.https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23056583/?tool=EBI |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Philipp Oberhettinger Monika Schütz Jack C Leo Nadja Heinz Jürgen Berger Ingo B Autenrieth Dirk Linke |
spellingShingle |
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. PLoS ONE |
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) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2012-01-01 |
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. |
url |
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23056583/?tool=EBI |
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