We demonstrate here that TLR5 recognizes a highly conserved structure that is particular to bacterial flagellin, and that this interaction is likely to be direct. This structure is required for ...

This shows the structure of bacterial flagellin protein bound to TLR5. Disclaimer: AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing ...

The structure of the flagellum differs ... There are also polymeric flagellin forms, which do not bind TLR5. Unlike the terminals, the central region of flagellin has higher sequence variation.

pylori and stomach cells activates a syringe-like pilus structure referred to ... CagL imitates a TLR5 recognition motif in the flagellin protein of other pathogens, thereby controlling the ...

One of these is Toll-like receptor 5 (TLR5): it binds flagellin, the protein that makes up the bacterial flagellum, which bacteria use to swim. Once bound to flagellin, TLR5 induces a pro-inflammatory ...

The scientists identified a new type of flagellin in the human gut, termed ‘silent flagellin’, that binds to the immune receptor Toll-like receptor 5 without inducing a pro-inflammatory response. The ...

The therapeutic potency of GP532 is expected not to be affected by neutralizing antibodies developing in humans following administration of the first generation TLR5 agonist entolimod, which has ...

Toll-like receptor 5 (TLR5), and the bacteria flagellin. Over the course of the study, mice exhibiting chronic skin inflammation were wounded on their side, resulting in tumors forming around the ...

termed ‘silent flagellin’, that binds to the immune receptor Toll-like receptor 5 without inducing a pro-inflammatory response. The findings provide a mechanism for the immune system to ...