ArticlePLoS pathogens2026
The host protein cyclophilin A restricts nuclear entry of HIV-1 mutants by reducing the elasticity of the viral capsid.
Article in PLoS pathogens, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Lenacapavir allosterically remodels the HIV-1 capsid.Science advances · 2026Article
- Viruses under mechanical force: Implications and applications.Virus research · 2026Review
- Stoichiometric binding of Cyclophilin-A to the HIV-1 capsid modulates its mechanoelastic properties.bioRxiv : the preprint server for biology · 2026Article
- All-atom molecular dynamics simulation of Cyclophilin A in complex with Sanglifehrin A.PloS one · 2026Article
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15 authors.
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Abstract
Binding of the host protein cyclophilin A (CypA) to the viral capsid exerts multiple effects on HIV-1 infection, including enhancement of reverse transcription, stabilization of the capsid, and promotion of nuclear entry. CypA can also inhibit infection of selected HIV-1 mutants by a poorly understood mechanism. Using atomic force microscopy methods, we previously showed that HIV-1 cores are highly elastic and that mutants with reduced capsid elasticity are impaired for nuclear entry and infection of nondividing cells. Here we demonstrate that binding of CypA to the capsids of such mutants inhibits their nuclear entry by further reducing the elasticity of their capsids. These effects were reversed by suppressor mutations that restored elasticity to the mutant capsids. Our results define the mechanism by which CypA controls HIV-1 nuclear entry. We hypothesize that nuclear entry involves temporal modulation of capsid elasticity by host proteins prior to and during passage through the nuclear pore.
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