ArticleiScience2026
Capsid and integrase play essential apposing roles in viral ribonucleoprotein assembly during HIV-1 core morphogenesis.
Article in iScience, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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8 authors.
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Abstract
HIV-1 virions harbor a core composed of a conical shell of capsid proteins that encases the viral ribonucleoprotein complex (vRNP). The vRNP is composed of HIV-1 genomic RNA (gRNA) and nucleocapsid (NC), reverse transcriptase (RT), and integrase (IN) proteins. Using a rapid affinity-capture purification approach, we have enriched for native HIV-1 capsids and analyzed the roles of IN-gRNA interactions and capsid lattice assembly on HIV-1 core formation. Following disruption of IN-gRNA interactions by allosteric IN inhibitor treatment or IN-deletion, we find that RT remains associated with cores that have effectively lost their IN, gRNA, and NC contents. Morphologically disrupted capsids formed by clinical inhibitor lenacapavir treatment or capsid hexamer cross-linking, by contrast, retained IN-gRNA but lost their RT and NC contents. These contrasting effects reveal that IN and the assembling capsid architecture cooperatively regulate the formation and encapsulation of vRNPs into the viral core during infectious HIV-1 morphogenesis.
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