1995
DOI: 10.1093/glycob/5.1.97
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A 23 kDa membrane glycoprotein bearing NeuNAcα2-3Galβ1-3GalNAc O-linked carbohydrate chains acts as a receptor for Streptococcus sanguis OMZ 9 on human buccal epithelial cells

Abstract: Streptococcus sanguis colonizes several human oral surfaces, including both hard and soft tissues. Large salivary mucin-like glycoproteins bearing sialic acid residues are known to bind various S.sanguis strains. However, the molecular basis for the adhesion of S.sanguis to human buccal epithelial cells (HBEC) has not been established. The present study shows that S.sanguis OMZ 9 binds to exfoliated HBEC in a sialic acid-sensitive manner. The desialylation of such cells invariably abolishes adhesion of S.sangu… Show more

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Cited by 40 publications
(25 citation statements)
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“…In that study, the interaction was localized to the amino-terminal portion of GPIb␣ (amino acids 1 to 225), suggesting that the epitopes on GPIb to which S. sanguis and S. gordonii adhere may be different. In a separate report, the O-linked trisaccharide NeuAc␣(2-3)Gal␤(1-3)GalNAc has been defined as a receptor for S. sanguis OMZ 9 on buccal epithelial cells (16). It would be interesting to determine whether S. sanguis OMZ 9 can also bind GPIb␣ and whether binding by these S. sanguis strains is mediated by a homologue of GspB and Hsa.…”
Section: Discussionmentioning
confidence: 99%
“…In that study, the interaction was localized to the amino-terminal portion of GPIb␣ (amino acids 1 to 225), suggesting that the epitopes on GPIb to which S. sanguis and S. gordonii adhere may be different. In a separate report, the O-linked trisaccharide NeuAc␣(2-3)Gal␤(1-3)GalNAc has been defined as a receptor for S. sanguis OMZ 9 on buccal epithelial cells (16). It would be interesting to determine whether S. sanguis OMZ 9 can also bind GPIb␣ and whether binding by these S. sanguis strains is mediated by a homologue of GspB and Hsa.…”
Section: Discussionmentioning
confidence: 99%
“…GMP also exhibits various antimicrobial and relatedactivities, including inhibiting influenza virus hemagglutination (Kawasaki et al, 1993), inhibiting the binding of cholera toxin (CT) and E. coli enterotoxins (Isoda et al, 1999Isoda, Kawasaki, Tanimoto, Dosako, & Idota, 1999Kawasaki et al, 1992;Neeser, Chambaz, Hoang, & LinkAmster, 1988) and inhibiting the growth of E. coli and various oral pathogens (Malkoski et al, 2001;Neeser, Chambaz, Del Vedovo, Prigent, & Guggenheim, 1988;Neeser et al, 1994Neeser et al, , 1995. In addition, Malkoski et al (2001) demonstrated that hydrolyzing GMP with endoproteinase Glu-C released various peptides, of which Ser (P) 149 k-casein f138-158 exhibited growth-inhibitory activity against Streptococcus mutans.…”
Section: Role In the Response To Infection And Diseasementioning
confidence: 99%
“…We showed that soluble caseinate and casein-derived glyco-and phosphopeptides behaved in vitro as potent inhibitors of Streptococcus sobrinus OMZ 176 adhesion to saliva-coated hydroxyapatite beads, whereas such molecules were not able to inhibit the attachment of Actinomyces viscosus Ny1 [Neeser et al, 1994]. Caseinoglycomacropeptide was also able to specifically prevent the adhesion in vitro of Streptococcus sanguis OMZ 9 to human buccal epithelial cells [Neeser et al, 1995], and casein-derived glyco-and phosphopeptides were observed to incorporate into the salivary pellicle inhibiting the adhesion of mutans streptococci [Schüpbach et al, 1996]. Thus, whilst the possible modulation of the oral microbiota by milk casein and/or some of its subcomponents has been documented, the in vivo significance remained to be investigated.…”
mentioning
confidence: 90%