Cloning and sequence analysis of flaA, a gene encoding a Spirochaeta aurantia flagellar filament surface antigen.
Spirochaeta aurantia DNA that coded for an antigenic determinant of the flagellin associated with the filament surface of the periplasmic flagella was isolated. When expressed in Escherichia coli, the antigenic polypeptide had an apparent molecular weight of 37,000. Sequence analysis of the antigen-encoding DNA revealed the presence of an open reading frame that determined a polypeptide with a predicted molecular weight of 31,241. This polypeptide showed a region of identity with the N-amino-terminal region of the 39,000- and 37,000-dalton flagellins of the distantly related spirochetes Treponema phagedenis and Treponema pallidum, respectively (S. J. Norris, N. W. Charon, R. G. Cook, M. D. Fuentes, and R. J. Limberger, J. Bacteriol. 170:4072-4082, 1988). The region of identity in the deduced S. aurantia polypeptide was preceded by a possible signal sequence and signal peptidase cleavage site.[1]References
- Cloning and sequence analysis of flaA, a gene encoding a Spirochaeta aurantia flagellar filament surface antigen. Brahamsha, B., Greenberg, E.P. J. Bacteriol. (1989) [Pubmed]
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