ArticleScience advances2026
Lenacapavir allosterically remodels the HIV-1 capsid.
Article in Science advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Structural basis of lenacapavir-induced HIV-1 capsid defects during virion maturation.Nature communications · 2026Article
- Capsid stabilization reprograms the nuclear fate of the HIV genome.Science advances · 2026Article
- Modeling Reveals How Direct-Acting Antivirals Redirect HBV Capsid Assembly Pathways to Noninfectious Products.bioRxiv : the preprint server for biology · 2026Article
- Damaging the conical morphology of HIV-1 capsid by targeting the FG-binding pocket and disfavoring pentameric subunits needed for core closure.bioRxiv : the preprint server for biology · 2026Article
- Mechanistic insights into lenacapavir-induced off-pathway HIV-1 capsid assembly.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Lenacapavir prevents production of infectious HIV-1 by abrogating immature virus assembly.bioRxiv : the preprint server for biology · 2026Article
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8 authors.
Funding
Abstract
Lenacapavir (LEN) is a highly potent, long-acting capsid inhibitor that holds exceptional promise for treatment and prevention of HIV-1 infection. LEN causes the mature viral capsid to rupture and lose integrity, but the underlying mechanism has been unclear. Here, we show that LEN is an allosteric modulator of HIV-1 capsid structure that fractures the capsid's fullerene cone architecture in two steps: initially by rupturing at high-curvature declinations, followed by fissuring of the capsid body. At the molecular level, LEN alters the noncovalent bonding interactions between capsid subunits and reduces local lattice curvature. We propose a stress-strain model to rationalize how LEN remodels HIV-1 capsid structure and thereby impairs the replication capacity of the virus.
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