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Last update 01 Nov 2024

HIV-1 Vif

Last update 01 Nov 2024

Basic Info

Synonyms-

Introduction-

Drugs associated with HIV-1 Vif

IMB-35

Target

HIV-1 Vif

Mechanism

HIV-1 Vif inhibitors

Active Org.

Institute of Pharmaceutical Biotechnology, Chinese Academy of Medical Sciences

Originator Org.

Institute of Pharmaceutical Biotechnology, Chinese Academy of Medical Sciences

Active Indication

HIV Infections

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

O2-16

Target

HIV-1 Vif

Mechanism

HIV-1 Vif inhibitors

Active Org.-

Originator Org.

OyaGen, Inc.

Active Indication-

Inactive Indication

HIV Infections

Drug Highest PhaseDiscontinued

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with HIV-1 Vif

100 Translational Medicine associated with HIV-1 Vif

0 Patents (Medical) associated with HIV-1 Vif

Literatures (Medical) associated with HIV-1 Vif

28 Feb 2023·mBio

A Virus-Packageable CRISPR System Identifies Host Dependency Factors Co-Opted by Multiple HIV-1 Strains

Article

Author: Montoya, Vanessa R. ; OhAinle, Molly ; Felton, Abby ; Emerman, Michael ; Ready, Trine M. ; Fine, Sydney R.

With a small genome of ~9.2 kb that encodes 14 major proteins, HIV must hijack host cellular machinery to successfully establish infection. These host proteins necessary for HIV replication are called “dependency factors.” Whole-genome, and then targeted screens were done to try to comprehensively identify all dependency factors acting throughout the HIV replication cycle.

01 Feb 2023·Biophysical Journal

Flexibility of the HIV Vif-A3F binding interaction

Article

Author: Alcantara, Juan ; Ball, K Aurelia ; Miller, Elizabeth

06 Jan 2023·Science Advances

Structural basis for HIV-1 antagonism of host APOBEC3G via Cullin E3 ligase

Article

Author: Zhou, Z. Hong ; Ito, Fumiaki ; Chen, Xiaojiang S. ; Yang, Hanjing ; Shiriaeva, Anna ; Liu, Shiheng ; Alvarez-Cabrera, Ana L.

Human APOBEC3G (A3G) is a virus restriction factor that inhibits HIV-1 replication and triggers lethal hypermutation on viral reverse transcripts. HIV-1 viral infectivity factor (Vif) breaches this host A3G immunity by hijacking a cellular E3 ubiquitin ligase complex to target A3G for ubiquitination and degradation. The molecular mechanism of A3G targeting by Vif-E3 ligase is unknown, limiting the antiviral efforts targeting this host-pathogen interaction crucial for HIV-1 infection. Here, we report the cryo–electron microscopy structures of A3G bound to HIV-1 Vif in complex with T cell transcription cofactor CBF-β and multiple components of the Cullin-5 RING E3 ubiquitin ligase. The structures reveal unexpected RNA-mediated interactions of Vif with A3G primarily through A3G’s noncatalytic domain, while A3G’s catalytic domain is poised for ubiquitin transfer. These structures elucidate the molecular mechanism by which HIV-1 Vif hijacks the host ubiquitin ligase to specifically target A3G to establish infection and offer structural information for the rational development of antiretroviral therapeutics.

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HIV-1 Vif

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