Atomic structure of the Campylobacter jejuni flagellar filament reveals how ε Proteobacteria escaped Toll-like receptor 5 surveillance
Abstract
Flagella are used by many pathogenic bacteria not only for motility but also for adhesion to host cells and to other bacteria in biofilm formation. Since thousands of copies of flagellin, the protein that forms the flagellar filament, are exposed on the surface of bacteria, they are a target for immune surveillance by hosts. Some bacteria important to human health, such as Campylobacter jejuni and Helicobacter pylori , have managed to evade the innate immune recognition of their flagellin. We show, with an atomic structure of the Campylobacter jejuni flagellar filament, how mutations that destabilize the filament in one region recognized by vertebrates have been compensated for by new contacts not seen in other flagellar filaments that would stabilize these filaments.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Jul 08, 2020
- Source ID
- 10.1073/pnas.2010996117
Entities
People
- Cheryl Ewing
- Edward H Egelman
- Fengbin Wang
- Frederic Poly
- Mark A. B. Kreutzberger
Organizations
- National Institute of General Medical Sciences
- Naval Medical Research Center
- United States Navy
- University of Virginia