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A stable immature lattice packages IP6 for HIV capsid maturation
Journal article   Open access   Peer reviewed

A stable immature lattice packages IP6 for HIV capsid maturation

Donna L. Mallery, Alex B. Kleinpeter, Nadine Renner, K. M. Rifat Faysal, Mariia Novikova, Leo Kiss, Miranda S. C. Wilson, Bilal Ahsan, Zunlong Ke, John A. G. Briggs, …
Science advances, Vol.7(11), eabe4716
03/01/2021
DOI: 10.1126/sciadv.abe4716
PMCID: PMC7946374
PMID: 33692109
url
https://doi.org/10.1126/sciadv.abe4716View
Published (Version of record) Open Access

Abstract

HIV immature lattice stability affects capsid maturation by altering IP 6 packaging. HIV virion assembly begins with the construction of an immature lattice consisting of Gag hexamers. Upon virion release, protease-mediated Gag cleavage leads to a maturation event in which the immature lattice disassembles and the mature capsid assembles. The cellular metabolite inositiol hexakisphosphate (IP 6 ) and maturation inhibitors (MIs) both bind and stabilize immature Gag hexamers, but whereas IP 6 promotes virus maturation, MIs inhibit it. Here we show that HIV is evolutionarily constrained to maintain an immature lattice stability that ensures IP 6 packaging without preventing maturation. Replication-deficient mutant viruses with reduced IP 6 recruitment display increased infectivity upon treatment with the MI PF46396 (PF96) or the acquisition of second-site compensatory mutations. Both PF96 and second-site mutations stabilise the immature lattice and restore IP 6 incorporation, suggesting that immature lattice stability and IP 6 binding are interdependent. This IP 6 dependence suggests that modifying MIs to compete with IP 6 for Gag hexamer binding could substantially improve MI antiviral potency.
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