TRIM5α association with cytoplasmic bodies is not required for antiretroviral activity

Byeongwoon Song, Felipe Diaz-Griffero, Do Hyun Park, Thomas Rogers, Matthew Stremlau, Joseph Sodroski

Research output: Contribution to journalArticle

49 Scopus citations

Abstract

The tripartite motif (TRIM) protein, TRIM5α, restricts infection by particular retroviruses. Many TRIM proteins form cytoplasmic bodies of unknown function. We investigated the relationship between cytoplasmic body formation and the structure and antiretroviral activity of TRIM5α. In addition to diffuse cytoplasmic staining, the TRIM5α proteins from several primate species were located in cytoplasmic bodies of different sizes; by contrast, TRIM5α from spider monkeys did not form cytoplasmic bodies. Despite these differences, all of the TRIM5α proteins exhibited the ability to restrict infection by particular retroviruses. Treatment of cells with geldanamycin, an Hsp90 inhibitor, resulted in disappearance or reduction of the TRIM5α-associated cytoplasmic bodies, yet exerted little effect on the restriction of retroviral infection. Studies of green fluorescent protein-TRIM5α fusion proteins indicated that no TRIM5α domain is specifically required for association with cytoplasmic bodies. Apparently, the formation of cytoplasmic bodies is not required for the antiretroviral activity of TRIM5α.

Original languageEnglish (US)
Pages (from-to)201-211
Number of pages11
JournalVirology
Volume343
Issue number2
DOIs
Publication statusPublished - Dec 20 2005

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Keywords

  • Cytoplasmic bodies
  • Cytoplasmic speckles
  • Geldanamycin
  • HIV-1
  • Restriction
  • Retrovirus
  • TRIM5α
  • Tripartite motif

ASJC Scopus subject areas

  • Virology

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