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Innate Immunity

Getting in TRIM to fight retroviruses

Nature Reviews Microbiology volume 6, page 797 (2008)Cite this article

Members of the TRIM family of proteins are involved in a range of cellular functions and typically contain a RING domain, one or more B-box domains and a coiled-coil region. As befits RING-domain containing proteins, several TRIMs have ubiquitin E3 ligase activity. B-box domains are zinc-finger motifs that are only found in TRIM proteins, whereas coiled-coil regions are often involved in protein oligomerization.

Many TRIM proteins also have a SPRY domain at their carboxyl terminus, which, in those TRIM proteins that are involved in innate immunity, determines their specificity for particular retroviruses. The mechanism of this antiviral function might involve ubiquitin ligase activity but TRIM proteins in which the RING domain has been removed still retain antiviral capacity, albeit a capacity that is reduced in strength. The coiled-coil, B-box and SPRY domains are essential for recognizing and combating viruses.

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References

ORIGINAL RESEARCH PAPER

  1. Kar, A. K., Diaz-Griffero, F., Li, Y., Li, X. & Sodroski, J. Biochemical and biophysical characterization of a chimeric TRIM21–TRIM5α protein. J. Virol. 17 Sep 2008 (doi:10.1128/JVI.01559-08)

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  2. Langelier, C. R. et al. Biochemical characterization of a recombinant TRIM5α protein that restricts HIV-1 replication J. Virol. 17 Sep 2008 (doi:10.1128/JVI.01562-08)

    Article  CAS  Google Scholar 

FURTHER READING

  1. Nisole, S., Stoye, J. P. & Saïb, A. TRIM family proteins: retroviral restriction and antiviral defence. Nature Rev. Microbiol. 3, 799–808 (2008)

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Authors
  1. Christopher Surridge
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Surridge, C. Getting in TRIM to fight retroviruses. Nat Rev Microbiol 6, 797 (2008). https://doi.org/10.1038/nrmicro2017

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  • DOI: https://doi.org/10.1038/nrmicro2017

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