Nef enhances HIV-1 infectivity via association with the virus assembly complex

Journal Article · Thu Apr 10 04:00:00 EDT 2008 · Virology

OSTI ID:21140968

Mingli, Qi ^[1]; Aiken, Christopher ^[1]

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1. Department of Microbiology and Immunology, Vanderbilt University School of Medicine, A-5301 Medical Center North, Nashville, TN 37232-2363 (United States)

The HIV-1 accessory protein Nef enhances virus infectivity by facilitating an early post-entry step of infection. Nef acts in the virus producer cell, leading to a beneficial modification to HIV-1 particles. Nef itself is incorporated into HIV-1 particles, where it is cleaved by the viral protease during virion maturation. To probe the role of virion-associated Nef in HIV-1 infection, we generated a fusion protein consisting of the host protein cyclophilin A (CypA) linked to the amino terminus of Nef. The resulting CypA-Nef protein enhanced the infectivity of Nef-defective HIV-1 particles and was specifically incorporated into the virions via association with Gag during particle assembly. Pharmacologic or genetic inhibition of CypA-Nef binding to Gag prevented incorporation of CypA-Nef into virions and inhibited infectivity enhancement. Our results indicate that infectivity enhancement by Nef requires its association with a component of the assembling HIV-1 particle.

• OSTI ID: 21140968
• Journal Information: Virology, Journal Name: Virology Journal Issue: 2 Vol. 373; ISSN VIRLAX; ISSN 0042-6822
• Country of Publication: United States
• Language: English

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