Cutting Edge: FimH Adhesin of Type 1 Fimbriae Is a Novel TLR4 Ligand | Zendy

Karen L. Mossman | Zendy; M. Firoz Mian | Zendy; Nicole M. Lauzon | Zendy; Carlton Gyles | Zendy; Brian D. Lichty | Zendy; Randy Mackenzie | Zendy; Navkiran Gill | Zendy; Ali A. Ashkar | Zendy

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Cutting Edge: FimH Adhesin of Type 1 Fimbriae Is a Novel TLR4 Ligand

Author(s) -

Karen L. Mossman,

M. Firoz Mian,

Nicole M. Lauzon,

Carlton Gyles,

Brian D. Lichty,

Randy Mackenzie,

Navkiran Gill,

Ali A. Ashkar

Publication year - 2008

Publication title -

the journal of immunology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.737

H-Index - 372

eISSN - 1550-6606

pISSN - 0022-1767

DOI - 10.4049/jimmunol.181.10.6702

Subject(s) - fimbria , bacterial adhesin , microbiology and biotechnology , ligand (biochemistry) , chemistry , fimbriae proteins , escherichia coli , biology , biochemistry , gene , receptor

Several TLR ligands of bacterial origin induce innate immune responses. Although FimH, the adhesin portion of type 1 fimbria, plays an important role in the pathogenicity of some gram-negative bacteria, its ability to stimulate the innate immune system via TLR signaling remains unclear. In this study we report that FimH induces potent innate responses in a MyD88-dependent fashion. The FimH-induced innate activity was restricted to cells expressing TLR4. In addition, FimH was able to bind directly to TLR4. More importantly, cells unresponsive to LPS were responsive to FimH and the presence or absence of MD-2 and CD14 had no effect on FimH activity. Our data suggest that TLR4 is a functional receptor for the adhesin portion of bacterial type 1 fimbria.

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