Escherichia coli O127 group 4 capsule proteins assemble at the outer membrane.

Enteropathogenic Escherichia coli O127 is encapsulated by a protective layer of polysaccharide made of the same strain specific O-antigen as the serotype lipopolysaccharide. Seven genes encoding capsule export functions comprise the group 4 capsule (gfc) operon. Genes gfcE, etk and etp encode homolo...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Matthew R Larson, Kassia Biddle, Adam Gorman, Sarah Boutom, Ilan Rosenshine, Mark A Saper
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/333b0ce93bb94bbeb53fe28f8142ebd6
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:333b0ce93bb94bbeb53fe28f8142ebd6
record_format	dspace
spelling	oai:doaj.org-article:333b0ce93bb94bbeb53fe28f8142ebd62021-12-02T20:13:06ZEscherichia coli O127 group 4 capsule proteins assemble at the outer membrane.1932-620310.1371/journal.pone.0259900https://doaj.org/article/333b0ce93bb94bbeb53fe28f8142ebd62021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0259900https://doaj.org/toc/1932-6203Enteropathogenic Escherichia coli O127 is encapsulated by a protective layer of polysaccharide made of the same strain specific O-antigen as the serotype lipopolysaccharide. Seven genes encoding capsule export functions comprise the group 4 capsule (gfc) operon. Genes gfcE, etk and etp encode homologs of the group 1 capsule secretion system but the upstream gfcABCD genes encode unknown functions specific to group 4 capsule export. We have developed an expression system for the large-scale production of the outer membrane protein GfcD. Contrary to annotations, we find that GfcD is a non-acylated integral membrane protein. Circular dichroism spectroscopy, light-scattering data, and the HHomp server suggested that GfcD is a monomeric β-barrel with 26 β-strands and an internal globular domain. We identified a set of novel protein-protein interactions between GfcB, GfcC, and GfcD, both in vivo and in vitro, and quantified the binding properties with isothermal calorimetry and biolayer interferometry. GfcC and GfcB form a high-affinity heterodimer with a KD near 100 nM. This heterodimer binds to GfcD (KD = 28 μM) significantly better than either GfcB or GfcC alone. These gfc proteins may form a complex at the outer membrane for group 4 capsule secretion or for a yet unknown function.Matthew R LarsonKassia BiddleAdam GormanSarah BoutomIlan RosenshineMark A SaperPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 11, p e0259900 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Matthew R Larson Kassia Biddle Adam Gorman Sarah Boutom Ilan Rosenshine Mark A Saper Escherichia coli O127 group 4 capsule proteins assemble at the outer membrane.
description	Enteropathogenic Escherichia coli O127 is encapsulated by a protective layer of polysaccharide made of the same strain specific O-antigen as the serotype lipopolysaccharide. Seven genes encoding capsule export functions comprise the group 4 capsule (gfc) operon. Genes gfcE, etk and etp encode homologs of the group 1 capsule secretion system but the upstream gfcABCD genes encode unknown functions specific to group 4 capsule export. We have developed an expression system for the large-scale production of the outer membrane protein GfcD. Contrary to annotations, we find that GfcD is a non-acylated integral membrane protein. Circular dichroism spectroscopy, light-scattering data, and the HHomp server suggested that GfcD is a monomeric β-barrel with 26 β-strands and an internal globular domain. We identified a set of novel protein-protein interactions between GfcB, GfcC, and GfcD, both in vivo and in vitro, and quantified the binding properties with isothermal calorimetry and biolayer interferometry. GfcC and GfcB form a high-affinity heterodimer with a KD near 100 nM. This heterodimer binds to GfcD (KD = 28 μM) significantly better than either GfcB or GfcC alone. These gfc proteins may form a complex at the outer membrane for group 4 capsule secretion or for a yet unknown function.
format	article
author	Matthew R Larson Kassia Biddle Adam Gorman Sarah Boutom Ilan Rosenshine Mark A Saper
author_facet	Matthew R Larson Kassia Biddle Adam Gorman Sarah Boutom Ilan Rosenshine Mark A Saper
author_sort	Matthew R Larson
title	Escherichia coli O127 group 4 capsule proteins assemble at the outer membrane.
title_short	Escherichia coli O127 group 4 capsule proteins assemble at the outer membrane.
title_full	Escherichia coli O127 group 4 capsule proteins assemble at the outer membrane.
title_fullStr	Escherichia coli O127 group 4 capsule proteins assemble at the outer membrane.
title_full_unstemmed	Escherichia coli O127 group 4 capsule proteins assemble at the outer membrane.
title_sort	escherichia coli o127 group 4 capsule proteins assemble at the outer membrane.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/333b0ce93bb94bbeb53fe28f8142ebd6
work_keys_str_mv	AT matthewrlarson escherichiacolio127group4capsuleproteinsassembleattheoutermembrane AT kassiabiddle escherichiacolio127group4capsuleproteinsassembleattheoutermembrane AT adamgorman escherichiacolio127group4capsuleproteinsassembleattheoutermembrane AT sarahboutom escherichiacolio127group4capsuleproteinsassembleattheoutermembrane AT ilanrosenshine escherichiacolio127group4capsuleproteinsassembleattheoutermembrane AT markasaper escherichiacolio127group4capsuleproteinsassembleattheoutermembrane
_version_	1718374814656233472

Escherichia coli O127 group 4 capsule proteins assemble at the outer membrane.

Ejemplares similares