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TLR5 takes aim at bacterial propeller

Nature Immunology volume 4, pages 1159–1160 (2003)Cite this article

The Toll-like receptor (TLR) family targets pathogen-derived molecules in regions unlikely to change under selection pressures. For TLR5, which recognizes the protein flagellin, the function of the targeting motif is key.

To discriminate nonself from self, the innate immune system uses a set of germline-encoded pattern-recognition receptors (PRRs) that recognize conserved microbial structures called pathogen-associated mole-cular patterns (PAMPs)1. In mice and humans, the Toll-like receptors (TLRs) form a family of ten members that typically represent such PRRs. TLRs are able to sense a plethora of PAMPs that are structurally unrelated. For example, TLR2 and TLR4 recognize sugar-bearing molecules (peptidoglycans and lipopolysaccharides, respectively), and TLR3 and TLR9 sense nucleic acids (double-stranded RNA and unmethylated CpG DNA). Unexpectedly, TLR5 recognizes a protein, flagellin, from both Gram-positive and Gram-negative bacteria2. The recognition of protein by PRRs was unexpected, as PAMPs are conserved, but proteins are notoriously easy to mutate in response to selection pressures. In this issue of Nature Immunology, Smith et al. provide an explanation to this conundrum by demonstrating that TLR5 recognizes the very same motif in flagellin that is also necessary for propulsion, which is required for successful propagation of the bacteria3.

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Figure 1: Bacteria swim by rotating a flagellum that is attached by a flexible hook to the 'motor', part of which is a disc contained in the membrane.

K.R.

References

  1. Janeway, C.A. Jr. Immunol. Today 13, 11–16 (1992).

    CAS  Article  Google Scholar 

  2. Hayashi, F. et al. Nature 410, 1099–1103 (2001).

    CAS  Article  Google Scholar 

  3. Smith, K.D. et al. Nat. Immunol. 4, 1247–1253 (2003).

    CAS  Article  Google Scholar 

  4. Akira, S. Curr. Opin. Immunol. 15, 5–11 (2003).

    CAS  Article  Google Scholar 

  5. Beutler, B. & Rietschel, E.T. Nat. Rev. Immunol. 3, 169–176 (2003).

    CAS  Article  Google Scholar 

  6. Bell, J.K. et al. Trends Immunol. 24, 528–33 (2003).

    CAS  Article  Google Scholar 

  7. Samatey, F.A. et al. Nature 410, 331–337 (2001).

    CAS  Article  Google Scholar 

  8. Zeng, H. et al. J. Immunol. 171, 3668–3674 (2003).

    CAS  Article  Google Scholar 

  9. Gomez-Gomez, L. & Boller, T. Trends Plant Sci. 7, 251–256 (2002).

    CAS  Article  Google Scholar 

  10. Weber, A.N. et al. Nat. Immunol. 4, 794–800 (2003).

    CAS  Article  Google Scholar 

Download references

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  1. Centre National de la Recherche Scientifique UPR9022, Institut de Biologie Moléculaire et Cellulaire, 15 rue René Descartes, Strasbourg, 67084, France

    Jean-Marc Reichhart

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  1. Jean-Marc Reichhart
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Reichhart, JM. TLR5 takes aim at bacterial propeller. Nat Immunol 4, 1159–1160 (2003). https://doi.org/10.1038/ni1203-1159

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