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Purification and Characterization of Fimbriae from Fimbriate Vibrio cholerae O1 Strain Bgd17

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Title: Purification and Characterization of Fimbriae from Fimbriate Vibrio cholerae O1 Strain Bgd17
Authors: Ehara, Masahiko / Iwami, Mamoru / Ichinose, Yoshio / Shimotori, Shoichi / Kangethe, Stanley K. / Nakamura, Satoshi
Issue Date: 20-Dec-1991
Publisher: 長崎大学熱帯医学研究所 / Institute of Tropical Medicine, Nagasaki University
Citation: 熱帯医学 Tropical medicine 33(4). p109-125, 1991
Abstract: Fimbrillin (or pilin) of Vibrio cholerae O1, purified both from an E1 Tor strain and a classical strain was shown to have the indentical N-terminal amino acid sequence which is extensively homologous to those of the N-methylphenyl alanine (NMePhe) pilin molecules and partly homologous to that of TcpA (Taylor et al., 1987; Show and Taylor, 1990). The N-terminal amino acid residue of the fimbrillin was modified and has not been determined. Haemagglutinin (HA) activities of the purified fimbriae were completely inhibited by D-mannnose and D-glucose, but not by L-fucose. Interestingly, pellicle formation of fimbriate cells was also inhibited by D-mannnose and D-glucose but not by L-fucose as shown previously. Based on the hypothesis that fimbriae of V. cholerae O1 function as the colonization factor and the cell associated haemagglutinin, this correlation in inhibition by monosaccharides between HA activity and pellicle formation strongly suggests that D-glucose in Oral Rehydration Salts (ORS, recommended for treatment by World Health Organization) can reduce the clinical symptom (diarrhoea) by inhibiting the colonization of vibrio cells to the epithelial cells of the upper small intestine. The presence of fimbrial antigens among enteropathogenic V. cholerae O1 strains was confirmed by western blot- and dot blot-analyses. The fimbrillin of the strain Bgd17 was shown to be a simple protein. Immunoelectron microscopy of the fimbriae with a specific monoclonal antibody revealed that fimbriae of V. cholerae O1 function as fimbrial adhesins necessary for the cell-cell interaction.
URI: http://hdl.handle.net/10069/4587
ISSN: 03855643
Type: Departmental Bulletin Paper
Appears in Collections:Volume 33, No. 4

Citable URI : http://hdl.handle.net/10069/4587

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