Cytoplasmic body component TRIM5α requires lipid-enriched microdomains for efficient HIV-1 restriction

Seiga Ohmine, Ryuta Sakuma, Toshie Sakuma, Tayaramma Thatava, Gonzalo P. Solis, Yasuhiro Ikeda

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


TRIM5α is a member of the tripartite motif (TRIM) family of proteins and affects both early and late phases of the retroviral life cycle. Although TRIM5α multimerizes to form cytoplasmic bodies, which are thought to play an important role in viral restriction, the identity of TRIM5α-containing cytoplasmic bodies remains elusive. To better understand TRIM5α cytoplasmic body constituents and the cellular proteins that could be involved in the TRIM5α-mediated antiviral activities, we sought TRIM5α-binding factors. We identified a lipid microdomain protein flotillin-1/Reggie-2 as an interacting partner of TRIM5α via co-immunoprecipitation. Immunohistochemistry studies confirmed the co-localization of rhesus monkey TRIM5α (TRIM5αrh) cytoplasmic bodies with flotillin-1/Reggie-2. Caveolin-1, another lipid microdomain- associated protein, also co-localized with TRIM5α cytoplasmic bodies. Intriguingly, disruption of cellular cholesterol by cyclodextrin perturbed TRIM5α cytoplasmic body formation. Furthermore, lipid starvation partially relieved the endogenous post-entry restriction of HIV-1 infection, which could be subsequently restored by lipid repletion. These observations indicate the involvement of cellular lipids in TRIM5α-mediated antiviral activities. Given that many viruses utilize cellular lipid microdomains for viral entry and assembly, it is plausible that lipid-enriched domains provide microenvironments where TRIM5α recognizes retroviral components.

Original languageEnglish (US)
Pages (from-to)34508-34517
Number of pages10
JournalJournal of Biological Chemistry
Issue number45
StatePublished - Nov 5 2010

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Cytoplasmic body component TRIM5α requires lipid-enriched microdomains for efficient HIV-1 restriction'. Together they form a unique fingerprint.

Cite this