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| Title | The structural mechanism of HIV-2 Vif antagonism of human APOBEC3H. |
|---|---|
| Journal, issue, pages | Nat Commun, Year 2026 |
| Publish date | Jun 29, 2026 |
 Authors | Yange Niu / Michelle Lilly / Estelle K Ronayne / Michael Emerman / Nicholas M Chesarino / John D Gross /  |
| PubMed Abstract | Human APOBEC3 (A3) proteins restrict retrovirus infection by inducing hypermutations in viral cDNA. To counteract this restriction, lentiviruses, such as HIV-1 and HIV-2 encode the viral infectivity ...Human APOBEC3 (A3) proteins restrict retrovirus infection by inducing hypermutations in viral cDNA. To counteract this restriction, lentiviruses, such as HIV-1 and HIV-2 encode the viral infectivity factor (Vif), which hijacks a host Cullin-RING E3 ubiquitin ligase complex to target A3 proteins for proteasomal degradation. Here, we present the cryo-EM structure of HIV-2 Vif in complex with human A3H and CBFβ. The structure reveals that A3H forms a dimer mediated by dsRNA where each A3H monomer directly interacts with an HIV-2 Vif and the host protein CBFβ. Both HIV-2 Vif-A3H and CBFβ-A3H interfaces are critical for A3H degradation. Notably, however, the HIV-2 Vif-A3H interface is entirely distinct from the previously determined cryo-EM structure of the HIV-1 Vif and A3H complex. These findings suggest that HIV-1 and HIV-2 Vif, which are the result of distinct cross-species transmissions from species with different A3H characteristics, have followed separate evolutionary trajectories to counteract human A3H. |
 External links | Nat Commun / PubMed:42373647 |
| Methods | EM (single particle) |
| Resolution | 3.2 Å |
| Structure data | EMDB-74939, PDB-9zy0: EMDB-74940, PDB-9zy1: |
| Chemicals |  ChemComp-ZN: |
| Source |
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 Keywords | ANTIVIRAL PROTEIN/RNA / HIV-2 / Vif / APOBEC3H / Antagonism / Ubiquitination / ANTIVIRAL PROTEIN / ANTIVIRAL PROTEIN-RNA complex |
homo sapiens (human)
human immunodeficiency virus 2