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

Qi M, Aiken C
Virology. 2008 373 (2): 287-97

PMID: 18191978 · PMCID: PMC2440657 · DOI:10.1016/j.virol.2007.12.001

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.

MeSH Terms (19)

Amino Acid Substitution Base Sequence Binding Sites Cell Line Cyclophilin A Cyclosporine DNA Primers gag Gene Products, Human Immunodeficiency Virus Genes, nef HeLa Cells HIV-1 Humans Multiprotein Complexes Mutation nef Gene Products, Human Immunodeficiency Virus Plasmids Recombinant Fusion Proteins Virulence Virus Assembly

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