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. 1985 Aug;50(2):431–437. doi: 10.1128/aem.50.2.431-437.1985

Evidence for Separate Adhesion Mechanisms for Hydrophilic and Hydrophobic Surfaces in Vibrio proteolytica

John H Paul 1,*, Wade H Jeffrey 1
PMCID: PMC238638  PMID: 16346861

Abstract

The proteolytic enzymes pronase, trypsin, and chymotrypsin and the surfactant Triton X-100 inhibited attachment of Vibrio proteolytica to the hydrophobic substratum polystyrene by >97%. These treatments had no effect on attachment to hydrophilic substrata such as glass or tissue culture dishes. Both pronase and Triton X-100 effected the removal of previously attached cells from polystyrene but not from hydrophilic surfaces. Removal of cells from polystyrene by pronase left material (which we have termed footprints) that stained with the protein-specific stain Hoechst 2495 but not with the DNA-specific stain Hoechst 33342. Pronase treatment also caused a significant decrease in cell surface hydrophobicity as determined by phase partitioning in hexane or petroleum ether. Collectively, these results imply the existence of separate mechanisms for the adhesion of V. proteolytica to hydrophilic and hydrophobic substrata and suggest a role for protein in the latter mechanism.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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