Evasion of Toll-like receptor 5 by flagellated bacteria
National Academies of Sciences, Engineering, and Medicine · University of Washington · +2 more institutions
Abstract
Toll-like receptor 5 (TLR5) recognizes an evolutionarily conserved site on bacterial flagellin that is required for flagellar filament assembly and motility. The alpha and epsilon Proteobacteria, including the important human pathogens Campylobacter jejuni, Helicobacter pylori, and Bartonella bacilliformis, require flagellar motility to efficiently infect mammalian hosts. In this study, we demonstrate that these bacteria make flagellin molecules that are not recognized by TLR5. We map the site responsible for TLR5 evasion to amino acids 89-96 of the N-terminal D1 domain, which is centrally positioned within the previously defined TLR5 recognition site. Salmonella flagellin is strongly recognized by TLR5, but…
Citation impact
- FWCI
- 21.70
- Percentile
- 100%
- References
- 47
Authors
7- EAErica Andersen‐NissenCorresponding
National Academies of Sciences, Engineering, and Medicine, University of Washington, Institute for Systems Biology, Institute for Biological Sciences
- KDKelly D. Smith
National Academies of Sciences, Engineering, and Medicine, University of Washington, Institute for Systems Biology, Institute for Biological Sciences
- KSKatie Strobe
National Academies of Sciences, Engineering, and Medicine, University of Washington, Institute for Systems Biology, Institute for Biological Sciences
- SLSara L. Rassoulian Barrett
National Academies of Sciences, Engineering, and Medicine, University of Washington, Institute for Systems Biology, Institute for Biological Sciences
- BTBrad T. Cookson
National Academies of Sciences, Engineering, and Medicine, University of Washington, Institute for Systems Biology, Institute for Biological Sciences
Topics & keywords
- TLR5
- Flagellin
- Biology
- Flagellum
- Microbiology
- Motility
- Bacteria
- Proteobacteria