A single amino acid of the human immunodeficiency virus type 2 capsid affects its replication in the presence of cynomolgus monkey and human TRIM5alphas

J Virol. 2007 Jul;81(13):7280-5. doi: 10.1128/JVI.00406-07. Epub 2007 May 2.

Abstract

Human immunodeficiency virus type 2 (HIV-2) strains vary widely in their abilities to grow in Old World monkey (OWM) cells such as those of cynomolgus monkeys (CM). We evaluated eight HIV-2 isolates for their sensitivities to CM TRIM5alpha, an anti-HIV factor in OWM cells. We found that different HIV-2 isolates showed differences in their sensitivities to CM TRIM5alpha. Sequence analysis showed that TRIM5alpha-sensitive viruses had proline at the 120th position of the capsid protein (CA), whereas TRIM5alpha-resistant viruses had either alanine or glutamine. Mutagenesis studies indicated that the single amino acid at the 120th position indeed affected the sensitivity of the virus to CM TRIM5alpha.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Substitution*
  • Animals
  • Antiviral Restriction Factors
  • Capsid* / metabolism
  • Carrier Proteins / genetics*
  • Carrier Proteins / metabolism
  • Cells, Cultured
  • DNA Mutational Analysis
  • HIV-2 / genetics*
  • HIV-2 / metabolism
  • Humans
  • Macaca fascicularis
  • Mutagenesis, Site-Directed
  • Mutation, Missense*
  • Tripartite Motif Proteins
  • Ubiquitin-Protein Ligases
  • Virus Replication / genetics*

Substances

  • Antiviral Restriction Factors
  • Carrier Proteins
  • Tripartite Motif Proteins
  • TRIM5 protein, human
  • Ubiquitin-Protein Ligases