This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Neeser, J R Articles by Guggenheim, B Search for Related Content PubMed PubMed Citation Articles by Neeser, J R Articles by Guggenheim, B

 Previous Article  |  Next Article 

Infect Immun. 1988 December; 56(12): 3201-3208

Specific and nonspecific inhibition of adhesion of oral actinomyces and streptococci to erythrocytes and polystyrene by caseinoglycopeptide derivatives.

Nestlé Research Centre, Nestec Limited, Lausanne, Switzerland.

ABSTRACT

Various caseinoglycopeptide derivatives prepared from mammalian milk were evaluated as inhibitors of hemagglutinations mediated by Actinomyces viscosus Ny1, Streptococcus sanguis OMZ9, and, for comparative purposes, plant lectins from Arachis hypogaea and Bauhinia purpurea. It was found that recognition of the beta-D-galactose-(1----3)-2-acetamido-2-deoxy-D-galactose carbohydrate chain by Actinomyces viscosus Ny1 organisms and Arachis hypogaea and B. purpurea agglutinins had similar structural requirements; in all cases, the desialylated bovine caseinoglycomacropeptide, on which several units of the above mentioned disaccharide are clustered, behaved as the most potent hemagglutination inhibitor. By contrast, none of the preparations tested inhibited erythrocyte agglutination by S. sanguis OMZ9. Thus, the desialylated bovine caseinoglycomacropeptide acts as a potent and specific inhibitor of oral Actinomyces adhesion to cell membranes (a soft surface) and could be used as a probe for the study of recognition mechanisms mediated by Actinomyces galactose-binding lectins. During the present study, both native and desialylated variants of the same bovine glycomacropeptide also totally prevented the adhesion of Actinomyces viscosus Ny1, S. sanguis OMZ9, and S. mutans OMZ176 to polystyrene surfaces. Comparative evaluations of various structurally different compounds gave the following results. Neither mono- nor disaccharides related to caseinoglycopeptide carbohydrates prevented adhesion; highly positively or negatively charged polypeptides and polysaccharides were either not or only moderately active. Besides these glycomacropeptides, an inhibitory activity was also exhibited by other mucin-type glycoproteins carrying short O-linked carbohydrate chains (including bovine submaxillary mucin), polyethylene glycol, and bovine serum albumin. Consequently, caseinoglycopeptide prevention of oral bacterial adhesion to polystyrene tubes (a hard surface) takes place with no species specificity and can be compared to nonspecific inhibition exhibited by various polymers with very different structural characteristics.

This article has been cited by other articles:

• Rhoades, J. R., Gibson, G. R., Formentin, K., Beer, M., Greenberg, N., Rastall, R. A. (2005). Caseinoglycomacropeptide Inhibits Adhesion of Pathogenic Escherichia coli Strains to Human Cells in Culture. J DAIRY SCI 88: 3455-3459 [Abstract] [Full Text]  
• Etzel, M. R. (2004). Manufacture and Use of Dairy Protein Fractions. J. Nutr. 134: 996S-1002S [Abstract] [Full Text]