TRPC1 participates in the HSV-1 infection process by facilitating viral entry

Autores
He, DongXu; Mao, AiQin; Li, YouRan; Tam, SiuCheung; Zheng, YongTang; Yao, XiaoQiang; Birnbaumer, Lutz; Ambudkar, Indu S.; Ma, Xin
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Mammalian transient receptor potential (TRP) channels are major components of Ca2+ signaling pathways and control a diversity of physiological functions. Here, we report a specific role for TRPC1 in the entry of herpes simplex virus type 1 (HSV-1) into cells. HSV-1-induced Ca2+ release and entry were dependent on Orai1, STIM1, and TRPC1. Inhibition of Ca2+ entry or knockdown of these proteins attenuated viral entry and infection. HSV-1 glycoprotein D interacted with the third ectodomain of TRPC1, and this interaction facilitated viral entry. Knockout of TRPC1 attenuated HSV-1-induced ocular abnormality and morbidity in vivo in TRPC1−/− mice. There was a strong correlation between HSV-1 infection and plasma membrane localization of TRPC1 in epithelial cells within oral lesions in buccal biopsies from HSV-1-infected patients. Together, our findings demonstrate a critical role for TRPC1 in HSV-1 infection and suggest the channel as a potential target for anti-HSV therapy.
Fil: He, DongXu. Jiangnan University; China
Fil: Mao, AiQin. Jiangnan University; China
Fil: Li, YouRan. Jiangnan University; China
Fil: Tam, SiuCheung. Chinese University Of Hong Kong; Hong Kong
Fil: Zheng, YongTang. Kunming Institute Of Zoology Chinese Academy Of Sciences; China
Fil: Yao, XiaoQiang. Chinese University Of Hong Kong; Hong Kong
Fil: Birnbaumer, Lutz. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Biomédicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Biomédicas; Argentina
Fil: Ambudkar, Indu S.. National Institute Of Dental And Craniofacial Research ; Estados Unidos
Fil: Ma, Xin. Jiangnan University; China
Materia
HSV-1-infected patients
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/170216
Acceder
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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling TRPC1 participates in the HSV-1 infection process by facilitating viral entryHe, DongXuMao, AiQinLi, YouRanTam, SiuCheungZheng, YongTangYao, XiaoQiangBirnbaumer, LutzAmbudkar, Indu S.Ma, XinHSV-1-infected patientshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Mammalian transient receptor potential (TRP) channels are major components of Ca2+ signaling pathways and control a diversity of physiological functions. Here, we report a specific role for TRPC1 in the entry of herpes simplex virus type 1 (HSV-1) into cells. HSV-1-induced Ca2+ release and entry were dependent on Orai1, STIM1, and TRPC1. Inhibition of Ca2+ entry or knockdown of these proteins attenuated viral entry and infection. HSV-1 glycoprotein D interacted with the third ectodomain of TRPC1, and this interaction facilitated viral entry. Knockout of TRPC1 attenuated HSV-1-induced ocular abnormality and morbidity in vivo in TRPC1−/− mice. There was a strong correlation between HSV-1 infection and plasma membrane localization of TRPC1 in epithelial cells within oral lesions in buccal biopsies from HSV-1-infected patients. Together, our findings demonstrate a critical role for TRPC1 in HSV-1 infection and suggest the channel as a potential target for anti-HSV therapy.Fil: He, DongXu. Jiangnan University; ChinaFil: Mao, AiQin. Jiangnan University; ChinaFil: Li, YouRan. Jiangnan University; ChinaFil: Tam, SiuCheung. Chinese University Of Hong Kong; Hong KongFil: Zheng, YongTang. Kunming Institute Of Zoology Chinese Academy Of Sciences; ChinaFil: Yao, XiaoQiang. Chinese University Of Hong Kong; Hong KongFil: Birnbaumer, Lutz. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Biomédicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Biomédicas; ArgentinaFil: Ambudkar, Indu S.. National Institute Of Dental And Craniofacial Research ; Estados UnidosFil: Ma, Xin. Jiangnan University; ChinaScience Advances is the American Association for the Advancement of Science2021-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/170216He, DongXu; Mao, AiQin; Li, YouRan; Tam, SiuCheung; Zheng, YongTang; et al.; TRPC1 participates in the HSV-1 infection process by facilitating viral entry; Science Advances is the American Association for the Advancement of Science; Science Advances; 6; 12; 3-2021; 1-122375-2548CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1126/sciadv.aaz3367info:eu-repo/semantics/altIdentifier/url/https://www.science.org/doi/epdf/10.1126/sciadv.aaz3367info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-11-12T09:59:24Zoai:ri.conicet.gov.ar:11336/170216instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-11-12 09:59:25.078CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv TRPC1 participates in the HSV-1 infection process by facilitating viral entry
title TRPC1 participates in the HSV-1 infection process by facilitating viral entry
spellingShingle TRPC1 participates in the HSV-1 infection process by facilitating viral entry
He, DongXu
HSV-1-infected patients
title_short TRPC1 participates in the HSV-1 infection process by facilitating viral entry
title_full TRPC1 participates in the HSV-1 infection process by facilitating viral entry
title_fullStr TRPC1 participates in the HSV-1 infection process by facilitating viral entry
title_full_unstemmed TRPC1 participates in the HSV-1 infection process by facilitating viral entry
title_sort TRPC1 participates in the HSV-1 infection process by facilitating viral entry
dc.creator.none.fl_str_mv He, DongXu
Mao, AiQin
Li, YouRan
Tam, SiuCheung
Zheng, YongTang
Yao, XiaoQiang
Birnbaumer, Lutz
Ambudkar, Indu S.
Ma, Xin
author He, DongXu
author_facet He, DongXu
Mao, AiQin
Li, YouRan
Tam, SiuCheung
Zheng, YongTang
Yao, XiaoQiang
Birnbaumer, Lutz
Ambudkar, Indu S.
Ma, Xin
author_role author
author2 Mao, AiQin
Li, YouRan
Tam, SiuCheung
Zheng, YongTang
Yao, XiaoQiang
Birnbaumer, Lutz
Ambudkar, Indu S.
Ma, Xin
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv HSV-1-infected patients
topic HSV-1-infected patients
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Mammalian transient receptor potential (TRP) channels are major components of Ca2+ signaling pathways and control a diversity of physiological functions. Here, we report a specific role for TRPC1 in the entry of herpes simplex virus type 1 (HSV-1) into cells. HSV-1-induced Ca2+ release and entry were dependent on Orai1, STIM1, and TRPC1. Inhibition of Ca2+ entry or knockdown of these proteins attenuated viral entry and infection. HSV-1 glycoprotein D interacted with the third ectodomain of TRPC1, and this interaction facilitated viral entry. Knockout of TRPC1 attenuated HSV-1-induced ocular abnormality and morbidity in vivo in TRPC1−/− mice. There was a strong correlation between HSV-1 infection and plasma membrane localization of TRPC1 in epithelial cells within oral lesions in buccal biopsies from HSV-1-infected patients. Together, our findings demonstrate a critical role for TRPC1 in HSV-1 infection and suggest the channel as a potential target for anti-HSV therapy.
Fil: He, DongXu. Jiangnan University; China
Fil: Mao, AiQin. Jiangnan University; China
Fil: Li, YouRan. Jiangnan University; China
Fil: Tam, SiuCheung. Chinese University Of Hong Kong; Hong Kong
Fil: Zheng, YongTang. Kunming Institute Of Zoology Chinese Academy Of Sciences; China
Fil: Yao, XiaoQiang. Chinese University Of Hong Kong; Hong Kong
Fil: Birnbaumer, Lutz. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Biomédicas. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones Biomédicas; Argentina
Fil: Ambudkar, Indu S.. National Institute Of Dental And Craniofacial Research ; Estados Unidos
Fil: Ma, Xin. Jiangnan University; China
description Mammalian transient receptor potential (TRP) channels are major components of Ca2+ signaling pathways and control a diversity of physiological functions. Here, we report a specific role for TRPC1 in the entry of herpes simplex virus type 1 (HSV-1) into cells. HSV-1-induced Ca2+ release and entry were dependent on Orai1, STIM1, and TRPC1. Inhibition of Ca2+ entry or knockdown of these proteins attenuated viral entry and infection. HSV-1 glycoprotein D interacted with the third ectodomain of TRPC1, and this interaction facilitated viral entry. Knockout of TRPC1 attenuated HSV-1-induced ocular abnormality and morbidity in vivo in TRPC1−/− mice. There was a strong correlation between HSV-1 infection and plasma membrane localization of TRPC1 in epithelial cells within oral lesions in buccal biopsies from HSV-1-infected patients. Together, our findings demonstrate a critical role for TRPC1 in HSV-1 infection and suggest the channel as a potential target for anti-HSV therapy.
publishDate 2021
dc.date.none.fl_str_mv 2021-03
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/170216
He, DongXu; Mao, AiQin; Li, YouRan; Tam, SiuCheung; Zheng, YongTang; et al.; TRPC1 participates in the HSV-1 infection process by facilitating viral entry; Science Advances is the American Association for the Advancement of Science; Science Advances; 6; 12; 3-2021; 1-12
2375-2548
CONICET Digital
CONICET
url http://hdl.handle.net/11336/170216
identifier_str_mv He, DongXu; Mao, AiQin; Li, YouRan; Tam, SiuCheung; Zheng, YongTang; et al.; TRPC1 participates in the HSV-1 infection process by facilitating viral entry; Science Advances is the American Association for the Advancement of Science; Science Advances; 6; 12; 3-2021; 1-12
2375-2548
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1126/sciadv.aaz3367
info:eu-repo/semantics/altIdentifier/url/https://www.science.org/doi/epdf/10.1126/sciadv.aaz3367
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Science Advances is the American Association for the Advancement of Science
publisher.none.fl_str_mv Science Advances is the American Association for the Advancement of Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.24909

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