HIV-1 adapts to lost IP6 coordination through second-site mutations that restore conical capsid assembly
Alex B. Kleinpeter; Donna L. Mallery; Nadine Renner; Anna Albecka; J Ole Klarhof; Eric O. Freed; Leo C. James · 2024 · Nature Communications
WASTE classifies this as Negative / Null Result Report · AI classification, approximate
The study found no significant effect — useful as a negative control or null benchmark for your own design.
Abstract
The HIV-1 capsid is composed of capsid (CA) protein hexamers and pentamers (capsomers) that contain a central pore hypothesised to regulate capsid assembly and facilitate nucleotide import early during post-infection. These pore functions are mediated by two positively charged rings created by CA Arg-18 (R18) and Lys-25 (K25). Here we describe the forced evolution of viruses containing mutations in R18 and K25. Whilst R18 mutants fail to replicate, K25A viruses acquire compensating mutations that restore nearly wild-type replication fitness. These compensating mutations, which rescue reverse t
Abstract by Alex B. Kleinpeter; Donna L. Mallery; Nadine Renner; Anna Albecka; J Ole Klarhof; Eric O. Freed; Leo C. James, Nature Communications (2024) — licensed CC BY 4.0.
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Metadata source: OpenAlex · DOI 10.1038/s41467-024-51971-w