Cloning and sequence analysis of flaA, a gene encoding a Spirochaeta aurantia flagellar filament surface antigen.
AUTOR(ES)
Brahamsha, B
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=209799Documentos Relacionados
- FlaA, a putative flagellar outer sheath protein, is not an immunodominant antigen associated with Lyme disease.
- Nucleotide sequence and analysis of a gene encoding anthranilate synthase component I in Spirochaeta aurantia.
- N-terminal amino acid sequences and amino acid compositions of the Spirochaeta aurantia flagellar filament polypeptides.
- The Spirochete FlaA Periplasmic Flagellar Sheath Protein Impacts Flagellar Helicity
- Structure and Expression of the FlaA Periplasmic Flagellar Protein of Borrelia burgdorferi