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Article

A second-site suppressor significantly improves the defective phenotype imposed by mutation of an aromatic residue in the N-terminal domain of the HIV-1 capsid protein.

Virology - 1 Mar 2007

Tang Shixing, Ablan Sherimay, Dueck Megan, Ayala-López Wilfredo, Soto Brenda, Caplan Margaret, Nagashima Kunio, Hewlett Indira K, Freed Eric O, Levin Judith G

Abstract excerpt

The HIV-1 capsid (CA) protein plays an important role in virus assembly and infectivity. Previously, we showed that Ala substitutions in the N-terminal residues Trp23 and Phe40 cause a severely defective phenotype. In searching for mutations at these positions that result in a non-lethal phenotype, we identified one candidate, W23F. Mutant virions contained aberrant cores, but unlike W23A, also displayed some...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 17055023
DOI: 10.1016/j.virol.2006.09.027
PMCID: PMC1851891

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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