Characterization of TRIM5α trimerization and its contribution to human immunodeficiency virus capsid binding

Hassan Javanbakht, Wen Yuan, Darwin F. Yeung, Byeongwoon Song, Felipe Diaz-Griffero, Yuan Li, Xing Li, Matthew Stremlau, Joseph Sodroski

Research output: Contribution to journalArticle

98 Scopus citations

Abstract

The coiled-coil domain of the tripartite motif (TRIM) family protein TRIM5α is required for trimerization and function as an antiretroviral restriction factor. Unlike the coiled-coil regions of other related TRIM proteins, the coiled coil of TRIM5α is not sufficient for multimerization. The linker region between the coiled-coil and B30.2 domains is necessary for efficient TRIM5α trimerization. Most of the hydrophilic residues predicted to be located on the surface-exposed face of the coiled coil can be altered without compromising TRIM5α antiviral activity against human immunodeficiency virus (HIV-1). However, changes that disrupt TRIM5α trimerization proportionately affect the ability of TRIM5α to bind HIV-1 capsid complexes. Therefore, TRIM5α trimerization makes a major contribution to its avidity for the retroviral capsid, and to the ability to restrict virus infection.

Original languageEnglish (US)
Pages (from-to)234-246
Number of pages13
JournalVirology
Volume353
Issue number1
DOIs
StatePublished - Sep 15 2006
Externally publishedYes

Keywords

  • Coiled-coil domain
  • HIV-1
  • Retroviral capsid
  • TRIM5α
  • Trimerization

ASJC Scopus subject areas

  • Virology

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    Javanbakht, H., Yuan, W., Yeung, D. F., Song, B., Diaz-Griffero, F., Li, Y., Li, X., Stremlau, M., & Sodroski, J. (2006). Characterization of TRIM5α trimerization and its contribution to human immunodeficiency virus capsid binding. Virology, 353(1), 234-246. https://doi.org/10.1016/j.virol.2006.05.017