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Innate mimicry

Nature Reviews Microbiology volume 6, page 329 (2008)Cite this article

A recent paper in Nature Medicine has identified a new class of virulence factor that bacterial pathogens use to interfere with Toll-like receptor (TLR) signalling.

The Toll–interleukin-1 receptor (TIR) domain is crucial for TLR function, and it has previously been suggested that competition for this key domain might be an efficient method of controlling TLR signalling. The authors began by searching databases for bacterial homologues of the human TIR domain. They identified two genes that encode TIR-domain-containing (Tcp) proteins, one (TcpB) in Brucella melitensis and the other (TcpC) in a uropathogenic Escherichia coli strain (E. coli CFT073). Analysis of the amino-acid sequence of these proteins showed that they have significant structural homology with the TIR domain of human TLR1. The TIR-homology domain is located in the carboxy-terminal region of each protein and contains the box 1 motif, which is essential for TLR signalling.

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References

ORIGINAL RESEARCH PAPER

  1. Cirl, C. et al. Subversion of Toll-like receptor signalling by a unique family of bacterial Toll/interleukin-1 receptor domain-containing proteins. Nature Med. 9 Mar 2008 (doi: 10.1038/nm1734)

FURTHER READING

  1. Salcedo, S. P. et al. Brucella control of dendritic cell maturation is dependent on the TIR-containing protein Btp1. PLoS Pathog. 4, e21 (2008)

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Authors
  1. Sheilagh Molloy
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Molloy, S. Innate mimicry. Nat Rev Microbiol 6, 329 (2008). https://doi.org/10.1038/nrmicro1903

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  • DOI: https://doi.org/10.1038/nrmicro1903

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