Rescue of bacterial motility using two- and three-species FliC chimeras.

ABSTRACT: The bacterial flagellar filament acts as a propeller to drive most bacterial swimming. The filament is made of flagellin, known as FliC in Escherichia coli. FliC consists of four domains, the highly conserved core D0 and D1 domains and the hypervariable outer D2 and D3 domains. The size and structure of the outer domains vary, being completely absent in some bacterial species. Here, we sought to identify outer domains from various species that are compatible with the ability of E. coli K-12 FliC to form filaments capable of supporting motility. We calculated a phylogeny of 210 representative flagellin amino acid sequences and generated a series of FliC variants, including outer domain-deleted forms and 11 chimeric FliC mutants using domains from E. coli K-12, Salmon

SUBMITTER: Scadden J 

PROVIDER: S-EPMC12445082 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature