Role of surface proteins in Vibrio cholerae attachment to chitin.
The role of surface proteins in Vibrio cholerae attachment to chitin particles in vitro was studied. Treatment of V. cholerae O1 ATCC 14034 and ATCC 14035 with pronase E reduced the attachment of bacteria to chitin particles by 57 to 77%. A statistically significant reduction was also observed when the attachment to chitin was evaluated in the presence of homologous Sarkosyl-insoluble membrane proteins (MPs) (67 to 84%), N-acetylglucosamine (GlcNAc) (62%), the sugar that makes up chitin, and wheat germ agglutinin (40 to 56%), a lectin that binds GlcNAc. The soluble oligomers N,N'-diacetylchitobiose or N,N', N"-triacetylchitotriose caused an inhibition of 14 to 23%. Sarkosyl-insoluble MPs able to bind chitin particles were isolated and visualized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis; two of these peptides (molecular sizes, 36 and 53 kDa) specifically bind GlcNAc.
Tarsi
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R
Institute of Microbiology, University of Ancona, 60131 Ancona, Italy.
Pruzzo
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C
D000117:Acetylglucosamine / Q000494:pharmacology; D001422:Bacterial Adhesion / Q000187:drug effects; D002686:Chitin / Q000502:physiology*; D004187:Disaccharides / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D008565:Membrane Proteins / Q000378:metabolism*; D010504:Periodic Acid / Q000494:pharmacology; D011402:Pronase / Q000378:metabolism; D014734:Vibrio cholerae / Q000502:physiology*; D014909:Wheat Germ Agglutinins / Q000494:pharmacology
D004187:Disaccharides; D008565:Membrane Proteins; D014909:Wheat Germ Agglutinins; D010504:Periodic Acid; D002686:Chitin; C032438:chitobiose; C009288:metaperiodate; D011402:Pronase; D000117:Acetylglucosamine