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


ABSTRACT: 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.

SUBMITTER: He D 

PROVIDER: S-EPMC7080438 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

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

He DongXu D   Mao AiQin A   Li YouRan Y   Tam SiuCheung S   Zheng YongTang Y   Yao XiaoQiang X   Birnbaumer Lutz L   Ambudkar Indu S IS   Ma Xin X  

Science advances 20200318 12


Mammalian transient receptor potential (TRP) channels are major components of Ca<sup>2+</sup> 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 Ca<sup>2+</sup> release and entry were dependent on Orai1, STIM1, and TRPC1. Inhibition of Ca<sup>2+</sup> entry or knockdown of these proteins attenuated viral entry and infection. HSV-1 glycoprotein D interacted w  ...[more]

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