Recruitment of the major vault protein by InlK: a Listeria monocytogenes strategy to avoid autophagy.

L. monocytogenes is a facultative intracellular bacterium responsible for listeriosis. It is able to invade, survive and replicate in phagocytic and non-phagocytic cells. The infectious process at the cellular level has been extensively studied and many virulence factors have been identified. Yet, t...

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Autores principales:	Laurent Dortet, Serge Mostowy, Ascel Samba-Louaka, Edith Gouin, Marie-Anne Nahori, Erik A C Wiemer, Olivier Dussurget, Pascale Cossart
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/4fc67258b10f4a9ebdd3a7a691e5d11f
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spelling	oai:doaj.org-article:4fc67258b10f4a9ebdd3a7a691e5d11f2021-11-18T06:03:08ZRecruitment of the major vault protein by InlK: a Listeria monocytogenes strategy to avoid autophagy.1553-73661553-737410.1371/journal.ppat.1002168https://doaj.org/article/4fc67258b10f4a9ebdd3a7a691e5d11f2011-08-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21829365/pdf/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374L. monocytogenes is a facultative intracellular bacterium responsible for listeriosis. It is able to invade, survive and replicate in phagocytic and non-phagocytic cells. The infectious process at the cellular level has been extensively studied and many virulence factors have been identified. Yet, the role of InlK, a member of the internalin family specific to L. monocytogenes, remains unknown. Here, we first show using deletion analysis and in vivo infection, that InlK is a bona fide virulence factor, poorly expressed in vitro and well expressed in vivo, and that it is anchored to the bacterial surface by sortase A. We then demonstrate by a yeast two hybrid screen using InlK as a bait, validated by pulldown experiments and immunofluorescence analysis that intracytosolic bacteria via an interaction with the protein InlK interact with the Major Vault Protein (MVP), the main component of cytoplasmic ribonucleoproteic particules named vaults. Although vaults have been implicated in several cellular processes, their role has remained elusive. Our analysis demonstrates that MVP recruitment disguises intracytosolic bacteria from autophagic recognition, leading to an increased survival rate of InlK over-expressing bacteria compared to InlK(-) bacteria. Together these results reveal that MVP is hijacked by L. monocytogenes in order to counteract the autophagy process, a finding that could have major implications in deciphering the cellular role of vault particles.Laurent DortetSerge MostowyAscel Samba-LouakaEdith GouinMarie-Anne NahoriErik A C WiemerOlivier DussurgetPascale CossartPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 7, Iss 8, p e1002168 (2011)
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 Laurent Dortet Serge Mostowy Ascel Samba-Louaka Edith Gouin Marie-Anne Nahori Erik A C Wiemer Olivier Dussurget Pascale Cossart Recruitment of the major vault protein by InlK: a Listeria monocytogenes strategy to avoid autophagy.
description	L. monocytogenes is a facultative intracellular bacterium responsible for listeriosis. It is able to invade, survive and replicate in phagocytic and non-phagocytic cells. The infectious process at the cellular level has been extensively studied and many virulence factors have been identified. Yet, the role of InlK, a member of the internalin family specific to L. monocytogenes, remains unknown. Here, we first show using deletion analysis and in vivo infection, that InlK is a bona fide virulence factor, poorly expressed in vitro and well expressed in vivo, and that it is anchored to the bacterial surface by sortase A. We then demonstrate by a yeast two hybrid screen using InlK as a bait, validated by pulldown experiments and immunofluorescence analysis that intracytosolic bacteria via an interaction with the protein InlK interact with the Major Vault Protein (MVP), the main component of cytoplasmic ribonucleoproteic particules named vaults. Although vaults have been implicated in several cellular processes, their role has remained elusive. Our analysis demonstrates that MVP recruitment disguises intracytosolic bacteria from autophagic recognition, leading to an increased survival rate of InlK over-expressing bacteria compared to InlK(-) bacteria. Together these results reveal that MVP is hijacked by L. monocytogenes in order to counteract the autophagy process, a finding that could have major implications in deciphering the cellular role of vault particles.
format	article
author	Laurent Dortet Serge Mostowy Ascel Samba-Louaka Edith Gouin Marie-Anne Nahori Erik A C Wiemer Olivier Dussurget Pascale Cossart
author_facet	Laurent Dortet Serge Mostowy Ascel Samba-Louaka Edith Gouin Marie-Anne Nahori Erik A C Wiemer Olivier Dussurget Pascale Cossart
author_sort	Laurent Dortet
title	Recruitment of the major vault protein by InlK: a Listeria monocytogenes strategy to avoid autophagy.
title_short	Recruitment of the major vault protein by InlK: a Listeria monocytogenes strategy to avoid autophagy.
title_full	Recruitment of the major vault protein by InlK: a Listeria monocytogenes strategy to avoid autophagy.
title_fullStr	Recruitment of the major vault protein by InlK: a Listeria monocytogenes strategy to avoid autophagy.
title_full_unstemmed	Recruitment of the major vault protein by InlK: a Listeria monocytogenes strategy to avoid autophagy.
title_sort	recruitment of the major vault protein by inlk: a listeria monocytogenes strategy to avoid autophagy.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/4fc67258b10f4a9ebdd3a7a691e5d11f
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Recruitment of the major vault protein by InlK: a Listeria monocytogenes strategy to avoid autophagy.

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