HIV-1 Accessory Protein Vpr Interacts with REAF/RPRD2 To Mitigate Its Antiviral Activity

Author:

Gibbons Joseph M.1,Marno Kelly M.1,Pike Rebecca1,Lee Wing-yiu Jason1,Jones Christopher E.1,Ogunkolade Babatunji W.1,Pardieu Claire1,Bryan Alexander2,Fu Rebecca Menhua2,Warnes Gary1,Rowley Paul A.3,Sloan Richard D.24,McKnight Áine1

Affiliation:

1. The Blizard Institute, Queen Mary University of London School of Medicine and Dentistry, London, United Kingdom

2. Infection Medicine, University of Edinburgh, Edinburgh, United Kingdom

3. Department of Biological Sciences, University of Idaho, Moscow, Idaho, USA

4. ZJU-UoE Institute, Zhejiang University, Jiaxing, Zhejiang, People’s Republic of China

Abstract

For at least 30 years, it has been known that HIV-1 Vpr, a protein carried in the virion, is important for efficient infection of primary macrophages. Vpr is also a determinant of the pathogenic effects of HIV-1 in vivo . A number of cellular proteins that interact with Vpr have been identified. So far, it has not been possible to associate these proteins with altered viral replication in macrophages or to explain why Vpr is carried in the virus particle. Here, we show that Vpr mitigates the antiviral effects of REAF, a protein highly expressed in primary macrophages and one that inhibits virus replication during reverse transcription. REAF is degraded by Vpr within 30 min of virus entry in a manner dependent on the nuclear localization of Vpr and its interaction with the cell’s protein degradation machinery.

Funder

Rosetrees Trust

UK Research and Innovation | Medical Research Council

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

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