TRIM5alpha

Curr Top Microbiol Immunol. 2009:339:47-66. doi: 10.1007/978-3-642-02175-6_3.

Abstract

TRIM5alpha protein blocks retroviral replication at early postentry stage reducing the accumulation of reverse transcriptase products. TRIM5alpha proteins of Old World primates restrict HIV-1 infection whereas TRIM5alpha proteins of most New World monkeys restrict SIV(mac) infection. TRIM5alpha protein has a RING domain, B-box 2 domain, coiled-coil domain, and PRYSPRY domain. The PRYSPRY domain of TRIM5alpha determines viral specificity and restriction potency by mediating recognition of the retroviral capsid. The coiled-coil domain is essential for TRIM5alpha oligomerization, which contributes to binding avidity for the viral capsid. The RING domain and B-box 2 domain are required for efficient restriction activity of TRIM5alpha protein but the mechanisms remain to be defined.

Publication types

  • Review

MeSH terms

  • Animals
  • Antiviral Restriction Factors
  • Carrier Proteins / chemistry
  • Carrier Proteins / physiology*
  • Cyclophilin A / physiology
  • DNA-(Apurinic or Apyrimidinic Site) Lyase / physiology
  • Humans
  • Mice
  • Proteasome Endopeptidase Complex / physiology
  • Proteins / chemistry
  • Proteins / genetics
  • Proteins / physiology*
  • Retroviridae Infections / prevention & control*
  • Tripartite Motif Proteins
  • Ubiquitin-Protein Ligases
  • Virus Internalization

Substances

  • Antiviral Restriction Factors
  • Carrier Proteins
  • Fv1 protein, mouse
  • Proteins
  • Tripartite Motif Proteins
  • TRIM5 protein, human
  • TRIM5(alpha) protein, rhesus monkey
  • Ubiquitin-Protein Ligases
  • Proteasome Endopeptidase Complex
  • APEX1 protein, human
  • DNA-(Apurinic or Apyrimidinic Site) Lyase
  • Cyclophilin A