A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection.

The mechanisms by which receptors guide intracellular virus transport are poorly characterized. The murine polyomavirus (Py) binds to the lipid receptor ganglioside GD1a and traffics to the endoplasmic reticulum (ER) where it enters the cytosol and then the nucleus to initiate infection. How Py reac...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Mengding Qian, Dawen Cai, Kristen J Verhey, Billy Tsai
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2009
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/01529c43d05943af82ac3cdb72d437d0
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:01529c43d05943af82ac3cdb72d437d0
record_format	dspace
spelling	oai:doaj.org-article:01529c43d05943af82ac3cdb72d437d02021-11-25T05:47:51ZA lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection.1553-73661553-737410.1371/journal.ppat.1000465https://doaj.org/article/01529c43d05943af82ac3cdb72d437d02009-06-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19503604/pdf/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374The mechanisms by which receptors guide intracellular virus transport are poorly characterized. The murine polyomavirus (Py) binds to the lipid receptor ganglioside GD1a and traffics to the endoplasmic reticulum (ER) where it enters the cytosol and then the nucleus to initiate infection. How Py reaches the ER is unclear. We show that Py is transported initially to the endolysosome where the low pH imparts a conformational change that enhances its subsequent ER-to-cytosol membrane penetration. GD1a stimulates not viral binding or entry, but rather sorting of Py from late endosomes and/or lysosomes to the ER, suggesting that GD1a binding is responsible for ER targeting. Consistent with this, an artificial particle coated with a GD1a antibody is transported to the ER. Our results provide a rationale for transport of Py through the endolysosome, demonstrate a novel endolysosome-to-ER transport pathway that is regulated by a lipid, and implicate ganglioside binding as a general ER targeting mechanism.Mengding QianDawen CaiKristen J VerheyBilly TsaiPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 5, Iss 6, p e1000465 (2009)
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 Mengding Qian Dawen Cai Kristen J Verhey Billy Tsai A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection.
description	The mechanisms by which receptors guide intracellular virus transport are poorly characterized. The murine polyomavirus (Py) binds to the lipid receptor ganglioside GD1a and traffics to the endoplasmic reticulum (ER) where it enters the cytosol and then the nucleus to initiate infection. How Py reaches the ER is unclear. We show that Py is transported initially to the endolysosome where the low pH imparts a conformational change that enhances its subsequent ER-to-cytosol membrane penetration. GD1a stimulates not viral binding or entry, but rather sorting of Py from late endosomes and/or lysosomes to the ER, suggesting that GD1a binding is responsible for ER targeting. Consistent with this, an artificial particle coated with a GD1a antibody is transported to the ER. Our results provide a rationale for transport of Py through the endolysosome, demonstrate a novel endolysosome-to-ER transport pathway that is regulated by a lipid, and implicate ganglioside binding as a general ER targeting mechanism.
format	article
author	Mengding Qian Dawen Cai Kristen J Verhey Billy Tsai
author_facet	Mengding Qian Dawen Cai Kristen J Verhey Billy Tsai
author_sort	Mengding Qian
title	A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection.
title_short	A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection.
title_full	A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection.
title_fullStr	A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection.
title_full_unstemmed	A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection.
title_sort	lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection.
publisher	Public Library of Science (PLoS)
publishDate	2009
url	https://doaj.org/article/01529c43d05943af82ac3cdb72d437d0
work_keys_str_mv	AT mengdingqian alipidreceptorsortspolyomavirusfromtheendolysosometotheendoplasmicreticulumtocauseinfection AT dawencai alipidreceptorsortspolyomavirusfromtheendolysosometotheendoplasmicreticulumtocauseinfection AT kristenjverhey alipidreceptorsortspolyomavirusfromtheendolysosometotheendoplasmicreticulumtocauseinfection AT billytsai alipidreceptorsortspolyomavirusfromtheendolysosometotheendoplasmicreticulumtocauseinfection AT mengdingqian lipidreceptorsortspolyomavirusfromtheendolysosometotheendoplasmicreticulumtocauseinfection AT dawencai lipidreceptorsortspolyomavirusfromtheendolysosometotheendoplasmicreticulumtocauseinfection AT kristenjverhey lipidreceptorsortspolyomavirusfromtheendolysosometotheendoplasmicreticulumtocauseinfection AT billytsai lipidreceptorsortspolyomavirusfromtheendolysosometotheendoplasmicreticulumtocauseinfection
_version_	1718414439735099392

A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection.

Ejemplares similares