Requirements for capsid-binding and an effector function in TRIMCyp-mediated restriction of HIV-1

Felipe Diaz-Griffero, Nick Vandegraaff, Yuan Li, Kathleen McGee-Estrada, Matthew Stremlau, Sohanya Welikala, Zhihai Si, Alan Engelman, Joseph Sodroski

Research output: Contribution to journalArticlepeer-review

79 Scopus citations


In owl monkeys, a retrotransposition event replaced the gene encoding the retroviral restriction factor TRIM5α with one encoding TRIMCyp, a fusion between the RING, B-box 2 and coiled-coil domains of TRIM5 and cyclophilin A. TRIMCyp restricts human immunodeficiency virus (HIV-1) infection by a mechanism dependent on the interaction of the cyclophilin A moiety and the HIV-1 capsid protein. Here, we show that infection by retroviruses other than HIV-1 can be restricted by TRIMCyp, providing an explanation for the evolutionary retention of the TRIMCyp gene in owl monkey lineages. The TRIMCyp-mediated block to HIV-1 infection occurs before the earliest step of reverse transcription. TRIMCyp-mediated restriction involves at least two functions: (1) capsid binding, which occurs most efficiently for trimeric TRIMCyp proteins that retain the coiled-coil and cyclophilin A domains, and (2) an effector function that depends upon the B-box 2 domain.

Original languageEnglish (US)
Pages (from-to)404-419
Number of pages16
Issue number2
StatePublished - Aug 1 2006
Externally publishedYes


  • Capsid
  • Cyclophilin
  • HIV
  • Restriction factors
  • Retrovirus
  • Reverse transcription
  • Tropism
  • Uncoating

ASJC Scopus subject areas

  • Virology


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