IFITM3 Reduces Retroviral Envelope Abundance and Function and Is Counteracted by glycoGag

Author:

Ahi Yadvinder S.1,Yimer Diborah1,Shi Guoli1,Majdoul Saliha1,Rahman Kazi1,Rein Alan1ORCID,Compton Alex A.1ORCID

Affiliation:

1. HIV Dynamics and Replication Program, Center for Cancer Research, National Cancer Institute, Frederick, Maryland, USA

Abstract

The viral envelope glycoprotein, known as “Env” in Retroviridae , is found on the virion surface and facilitates virus entry into cells by mediating cell attachment and fusion. Env is a major structural component of retroviruses and is targeted by all arms of the immune response, including adaptive and innate immunity. Less is known about how cell-intrinsic immunity prevents retrovirus replication at the level of individual cells. Here, we show that cellular IFITM3 and IFITM2 inhibit the fusion potential of retroviral virions by inhibiting Env protein via a two-pronged mechanism. IFITM proteins inhibit Env abundance in cells and also impair its function when levels are low. The posttranslational block of retroviral Env function by IFITM proteins is likely to impede both exogenous and endogenous retrovirus replication. In support of a relevant role for IFITM3 in retrovirus control, the retroviral accessory protein glycoGag counteracts IFITM3 function to promote virus infectivity.

Funder

Intramural Research Program of the National Institutes of Health

Publisher

American Society for Microbiology

Subject

Virology,Microbiology

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