Disease relevance of fliL

• The findings imply that although the signals for control of chemotaxis may be distinctly different in spirochetes, at least some of the molecules involved in torque generation, control of flagellar rotation and signal transduction are highly conserved with other bacteria [1].
• Nucleotide sequence analysis of a clone expressing three immunoreactive antigens has revealed the presence of an open reading frame highly homologous to the flagellar switch/motor protein, FliG, which is known to be essential for flagellar assembly and rotation, and chemotaxis in enteric bacteria [1].
• Antigenic behaviors of two axial flagellar proteins detected in Treponema denticola [2].
• The deduced amino acid sequences of FliQ, FliR, FlhB and FlhA' have significant homology with bacterial proteins associated with the flagellar export apparatus, whereas the deduced amino acid sequence of Orf1 has homology with an E. coli alcohol dehydrogenase [3].

High impact information on fliL

• Deletion of fliG resulted in a nonmotile mutant with a markedly decreased number of flagellar filaments [4].
• The cellular reversal frequency, however, was severely reduced, indicating that CheA in T. denticola mainly controls cellular reversal and that active chemotaxis signaling input is not required for coordination of flagellar rotation at both cell poles [5].
• The flagellar cytoskeleton of the spirochetes [6].

References