Identification of conserved domains in Salmonella muenchen flagellin that are essential for its ability to activate TLR5 and to induce an inflammatory response in vitro.

@article{Murthy2004IdentificationOC,
  title={Identification of conserved domains in Salmonella muenchen flagellin that are essential for its ability to activate TLR5 and to induce an inflammatory response in vitro.},
  author={Kanneganti G. K. Murthy and Amitabha Deb and Sunali D. Goonesekera and Csaba Szab{\'o} and Andrew L. Salzman},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 7},
  pages={5667-75}
}
The bacterial surface protein flagellin is widely distributed and well conserved among distant bacterial species. We and other investigators have reported recently that purified flagellin from Salmonella dublin or recombinant flagellin of Salmonella muenchen origin binds to the eukaryotic toll receptor TLR5 and activates the nuclear translocation of NF-kappaB and mitogen-activated protein kinase, resulting in the release of a host of pro-inflammatory mediators in vitro and in vivo. The amino… CONTINUE READING

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