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Updated: Apr 25, 2026

Assembly and Purification of Prototype Foamy Virus Intasomes
Published on: March 19, 2018
Structural insights for HIV-1 therapeutic strategies targeting Vif
Jason D Salter1, Guillermo A Morales2, Harold C Smith3
1OyaGen, Inc, 77 Ridgeland Road, Rochester, NY 14623, USA.
Abstract:
HIV-1 viral infectivity factor (Vif) is a viral accessory protein that is required for HIV-1 infection due largely to its role in recruiting antiretroviral factors of the APOBEC3 (apolipoprotein B editing catalytic subunit-like 3) family to an E3 ubiquitin ligase complex for polyubiquitylation and proteasomal degradation. The crystal structure of the (near) full-length Vif protein in complex with Elongin (Elo)B/C, core-binding factor (CBF)β and Cullin (Cul)5 revealed that Vif has a novel structural fold. In our opinion the structural data revealed not only the protein-protein interaction sites that determine Vif stability and interaction with cellular proteins, but also motifs driving Vif homodimerization, which are essential in Vif functionality and HIV-1 infection. Vif-mediated protein-protein interactions are excellent targets for a new class of antiretroviral therapeutics to combat AIDS.
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