ArticleRetrovirology2013
High level of susceptibility to human TRIM5α conferred by HIV-2 capsid sequences.
Article in Retrovirology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Article
- Structural insights into HIV-2 CA lattice formation and FG-pocket binding revealed by single-particle cryo-EM.Cell reports · 2025Article
- Intrahost evolution of the HIV-2 capsid correlates with progression to AIDS.Virus evolution · 2022Article
- HIV-1 capsid variability: viral exploitation and evasion of capsid-binding molecules.Retrovirology · 2021Review
- Toward a Macaque Model of HIV-1 Infection: Roadblocks, Progress, and Future Strategies.Frontiers in microbiology · 2020Review
- Delayed disease progression in HIV-2: the importance of TRIM5α and the retroviral capsid.Clinical and experimental immunology · 2019Review
- Limited HIV-2 reservoirs in central-memory CD4 T-cells associated to CXCR6 co-receptor expression in attenuated HIV-2 infection.PLoS pathogens · 2019Article
- Cyclophilins and nucleoporins are required for infection mediated by capsids from circulating HIV-2 primary isolates.Scientific reports · 2017Article
- Insight into HIV-2 latency may disclose strategies for a cure for HIV-1 infection.Journal of virus eradication · 2017Article
- Metabolic profiling during HIV-1 and HIV-2 infection of primary human monocyte-derived macrophages.Virology · 2016Article
- Heterogeneous susceptibility of circulating SIV isolate capsids to HIV-interacting factors.Retrovirology · 2013Article
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Authors and funding
8 authors.
Funding
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Abstract
backgroundHIV-2, which was transmitted to humans from a distant primate species (sooty mangabey), differs remarkably from HIV-1 in its infectivity, transmissibility and pathogenicity. We have tested the possibility that a greater susceptibility of HIV-2 capsid (CA) to the human restriction factor TRIM5α (hTRIM5α) could contribute to these differences.
resultsWe constructed recombinant clones expressing CA from a variety of HIV-2 viruses in the context of HIV-1 NL4-3-luciferase. CA sequences were amplified from the plasma of HIV-2 infected patients, including 8 subtype A and 7 subtype B viruses. CA from 6 non-epidemic HIV-2 subtypes, 3 HIV-2 CRF01_AB recombinants and 4 SIVsmm viruses were also tested. Susceptibility to hTRIM5α was measured by comparing single-cycle infectivity in human target cells expressing hTRIM5α to that measured in cells in which hTRIM5α activity was inhibited by overexpression of hTRIM5γ.The insertion of HIV-2 CA sequences in the context of HIV-1 did not affect expression and maturation of the HIV-2 CA protein. The level of susceptibility hTRIM5α expressed by viruses carrying HIV-2 CA sequences was up to 9-fold higher than that of HIV-1 NL4-3 and markedly higher than a panel of primary HIV-1 CA sequences. This phenotype was found both for viruses carrying CA from primary HIV-2 sequences and viruses carrying CA from laboratory-adapted HIV-2 clones. High hTRIM5α susceptibility was found in all HIV-2 subtypes. In this series of viruses, susceptibility to hTRIM5α was not significantly affected by the presence of a proline at position 119 or by the number of prolines at positions 119, 159 or 178 in HIV-2 CA. No significant correlation was found between HIV-2 viremia and sensitivity to hTRIM5α.
conclusionsHIV-2 capsid sequences expressed high levels of susceptibility to hTRIM5α. This property, common to all HIV-2 sequences tested, may contribute in part to the lower replication and pathogenicity of this virus in humans.
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