The virulence protein SopD2 regulates membrane dynamics of Salmonella-containing vacuoles.

Salmonella enterica serovar Typhimurium is a Gram-negative bacterial pathogen causing gastroenteritis in humans and a systemic typhoid-like illness in mice. The capacity of Salmonella to cause diseases relies on the establishment of its intracellular replication niche, a membrane-bound compartment n...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Nina Schroeder, Thomas Henry, Chantal de Chastellier, Weidong Zhao, Aude-Agnès Guilhon, Jean-Pierre Gorvel, Stéphane Méresse
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2010
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/c2067ce942964972a3416e439ab40145
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:c2067ce942964972a3416e439ab40145
record_format	dspace
spelling	oai:doaj.org-article:c2067ce942964972a3416e439ab401452021-12-02T20:00:28ZThe virulence protein SopD2 regulates membrane dynamics of Salmonella-containing vacuoles.1553-73661553-737410.1371/journal.ppat.1001002https://doaj.org/article/c2067ce942964972a3416e439ab401452010-07-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20664790/pdf/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Salmonella enterica serovar Typhimurium is a Gram-negative bacterial pathogen causing gastroenteritis in humans and a systemic typhoid-like illness in mice. The capacity of Salmonella to cause diseases relies on the establishment of its intracellular replication niche, a membrane-bound compartment named the Salmonella-containing vacuole (SCV). This requires the translocation of bacterial effector proteins into the host cell by type three secretion systems. Among these effectors, SifA is required for the SCV stability, the formation of Salmonella-induced filaments (SIFs) and plays an important role in the virulence of Salmonella. Here we show that the effector SopD2 is responsible for the SCV instability that triggers the cytoplasmic release of a sifA(-) mutant. Deletion of sopD2 also rescued intra-macrophagic replication and increased virulence of sifA(-) mutants in mice. Membrane tubular structures that extend from the SCV are the hallmark of Salmonella-infected cells. Until now, these unique structures have not been observed in the absence of SifA. The deletion of sopD2 in a sifA(-) mutant strain re-established membrane trafficking from the SCV and led to the formation of new membrane tubular structures, the formation of which is dependent on other Salmonella effector(s). Taken together, our data demonstrate that SopD2 inhibits the vesicular transport and the formation of tubules that extend outward from the SCV and thereby contributes to the sifA(-) associated phenotypes. These results also highlight the antagonistic roles played by SopD2 and SifA in the membrane dynamics of the vacuole, and the complex actions of SopD2, SifA, PipB2 and other unidentified effector(s) in the biogenesis and maintenance of the Salmonella replicative niche.Nina SchroederThomas HenryChantal de ChastellierWeidong ZhaoAude-Agnès GuilhonJean-Pierre GorvelStéphane MéressePublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 6, Iss 7, p e1001002 (2010)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Nina Schroeder Thomas Henry Chantal de Chastellier Weidong Zhao Aude-Agnès Guilhon Jean-Pierre Gorvel Stéphane Méresse The virulence protein SopD2 regulates membrane dynamics of Salmonella-containing vacuoles.
description	Salmonella enterica serovar Typhimurium is a Gram-negative bacterial pathogen causing gastroenteritis in humans and a systemic typhoid-like illness in mice. The capacity of Salmonella to cause diseases relies on the establishment of its intracellular replication niche, a membrane-bound compartment named the Salmonella-containing vacuole (SCV). This requires the translocation of bacterial effector proteins into the host cell by type three secretion systems. Among these effectors, SifA is required for the SCV stability, the formation of Salmonella-induced filaments (SIFs) and plays an important role in the virulence of Salmonella. Here we show that the effector SopD2 is responsible for the SCV instability that triggers the cytoplasmic release of a sifA(-) mutant. Deletion of sopD2 also rescued intra-macrophagic replication and increased virulence of sifA(-) mutants in mice. Membrane tubular structures that extend from the SCV are the hallmark of Salmonella-infected cells. Until now, these unique structures have not been observed in the absence of SifA. The deletion of sopD2 in a sifA(-) mutant strain re-established membrane trafficking from the SCV and led to the formation of new membrane tubular structures, the formation of which is dependent on other Salmonella effector(s). Taken together, our data demonstrate that SopD2 inhibits the vesicular transport and the formation of tubules that extend outward from the SCV and thereby contributes to the sifA(-) associated phenotypes. These results also highlight the antagonistic roles played by SopD2 and SifA in the membrane dynamics of the vacuole, and the complex actions of SopD2, SifA, PipB2 and other unidentified effector(s) in the biogenesis and maintenance of the Salmonella replicative niche.
format	article
author	Nina Schroeder Thomas Henry Chantal de Chastellier Weidong Zhao Aude-Agnès Guilhon Jean-Pierre Gorvel Stéphane Méresse
author_facet	Nina Schroeder Thomas Henry Chantal de Chastellier Weidong Zhao Aude-Agnès Guilhon Jean-Pierre Gorvel Stéphane Méresse
author_sort	Nina Schroeder
title	The virulence protein SopD2 regulates membrane dynamics of Salmonella-containing vacuoles.
title_short	The virulence protein SopD2 regulates membrane dynamics of Salmonella-containing vacuoles.
title_full	The virulence protein SopD2 regulates membrane dynamics of Salmonella-containing vacuoles.
title_fullStr	The virulence protein SopD2 regulates membrane dynamics of Salmonella-containing vacuoles.
title_full_unstemmed	The virulence protein SopD2 regulates membrane dynamics of Salmonella-containing vacuoles.
title_sort	virulence protein sopd2 regulates membrane dynamics of salmonella-containing vacuoles.
publisher	Public Library of Science (PLoS)
publishDate	2010
url	https://doaj.org/article/c2067ce942964972a3416e439ab40145
work_keys_str_mv	AT ninaschroeder thevirulenceproteinsopd2regulatesmembranedynamicsofsalmonellacontainingvacuoles AT thomashenry thevirulenceproteinsopd2regulatesmembranedynamicsofsalmonellacontainingvacuoles AT chantaldechastellier thevirulenceproteinsopd2regulatesmembranedynamicsofsalmonellacontainingvacuoles AT weidongzhao thevirulenceproteinsopd2regulatesmembranedynamicsofsalmonellacontainingvacuoles AT audeagnesguilhon thevirulenceproteinsopd2regulatesmembranedynamicsofsalmonellacontainingvacuoles AT jeanpierregorvel thevirulenceproteinsopd2regulatesmembranedynamicsofsalmonellacontainingvacuoles AT stephanemeresse thevirulenceproteinsopd2regulatesmembranedynamicsofsalmonellacontainingvacuoles AT ninaschroeder virulenceproteinsopd2regulatesmembranedynamicsofsalmonellacontainingvacuoles AT thomashenry virulenceproteinsopd2regulatesmembranedynamicsofsalmonellacontainingvacuoles AT chantaldechastellier virulenceproteinsopd2regulatesmembranedynamicsofsalmonellacontainingvacuoles AT weidongzhao virulenceproteinsopd2regulatesmembranedynamicsofsalmonellacontainingvacuoles AT audeagnesguilhon virulenceproteinsopd2regulatesmembranedynamicsofsalmonellacontainingvacuoles AT jeanpierregorvel virulenceproteinsopd2regulatesmembranedynamicsofsalmonellacontainingvacuoles AT stephanemeresse virulenceproteinsopd2regulatesmembranedynamicsofsalmonellacontainingvacuoles
_version_	1718375746796257280

The virulence protein SopD2 regulates membrane dynamics of Salmonella-containing vacuoles.

Ejemplares similares