%0 Electronic Article %A Ge, Y and Charon, N W %I American Society for Microbiology %D 1997 %D 1997 %G English %@ 0021-9193 %@ 1098-5530 %~ Katalog der Westsächsischen Hochschule Zwickau %T An unexpected flaA homolog is present and expressed in Borrelia burgdorferi %V 179 %J Journal of Bacteriology %V 179 %N 2 %P 552-556 %U http://dx.doi.org/10.1128/jb.179.2.552-556.1997 %X Most investigators have assumed that the periplasmic flagella (PFs) of Borrelia burgdorferi are composed of only one flagellin protein. The PFs of most other spirochete species are complex: these PFs contain an outer sheath of FlaA proteins and a core filament of FlaB proteins. During an analysis of a chemotaxis gene cluster of B. burgdorferi 212, we were surprised to find a flaA gene homolog with a deduced polypeptide having 54 to 58% similarity to FlaA from other spirochetes. Like other FlaA proteins, B. burgdorferi FlaA has a conserved signal sequence at its N terminus. Based on reverse transcription-PCR and primer extension analysis, this flaA homolog and five chemotaxis genes constitute a motility-chemotaxis operon. Immunoblots using anti-FlaA serum from Treponema pallidum and a lysate of B. burgdorferi showed strong reactivity to a protein of 38.0 kDa, which is consistent with the expression of flaA in growing cells. %Z https://www.katalog.fh-zwickau.de/Record/ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9qYi4xNzkuMi41NTItNTU2LjE5OTc %U https://www.katalog.fh-zwickau.de/Record/ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9qYi4xNzkuMi41NTItNTU2LjE5OTc