Purification and characterization of the fimbria F18ac (2134P) isolated from enterotoxigenic Escherichia coli (ETEC).
The adhesin F18ac purified on Sepharose CL 4B column chromatography and SDS-PAGE stained with Coomassie Blue and Western blotting using specific anti-F18ac serum presented one band of approximately 17kDa. Gold immunolabeling revealed that the adhesin F18ac has a fimbrial structure on the bacterial surface. The first 27 amino acid residues of the N-terminal portion of the adhesin F18ac, showed 92.5% homology (25 amino acids) with the F107 (F18ab) fimbriae.
Departamento de Bioquímica, I.B., UNICAMP, 13081-970, Campinas, S.P. Brazil.
C R
CR
Amorim
M S
MS
Matsuura
J C
JC
Rosa
L J
LJ
Greene
D S
DS
Leite
T
T
Yano
D018830:Adhesins, Escherichia coli / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western / Q000662:veterinary; D002850:Chromatography, Gel / Q000662:veterinary; D004591:Electrophoresis, Polyacrylamide Gel / Q000662:veterinary; D004926:Escherichia coli / Q000737:chemistry*; D010861:Fimbriae, Bacterial / Q000737:chemistry*; D008969:Molecular Sequence Data; D013552:Swine
D018830:Adhesins, Escherichia coli