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Applied and Environmental Microbiology, March 1999, p. 1348-1351, Vol. 65, No. 3
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Role of Surface Proteins in Vibrio cholerae Attachment to Chitin

Renato Tarsi and Carla Pruzzo*

Institute of Microbiology, University of Ancona, 60131 Ancona, Italy

Received 8 June 1998/Accepted 8 December 1998

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.

* Corresponding author. Mailing address: Institute of Microbiology, University of Ancona, Via Ranieri Monte D'Ago, 60131 Ancona, Italy. Phone: 390712204697. Fax: 390712204693. E-mail: pruzzo{at}mbox.ulisse.it.

Applied and Environmental Microbiology, March 1999, p. 1348-1351, Vol. 65, No. 3
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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Copyright © 1999 by the American Society for Microbiology. All rights reserved.