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Infect Immun, April 1998, p. 1439-1444, Vol. 66, No. 4
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Adherence of Streptococcus pneumoniae to Respiratory Epithelial Cells Is Inhibited by Sialylated Oligosaccharides

Roger Barthelson,* Ali Mobasseri, David Zopf, and Paul Simon

Neose Technologies, Inc., Horsham, Pennsylvania 19044

Received 6 October 1997/Returned for modification 18 November 1997/Accepted 12 January 1998

To study carbohydrate-mediated adherence of Streptococcus pneumoniae to the human airway, we measured binding of live S. pneumoniae organisms to a cultured cell line derived from the lining of the conjunctiva and to primary monolayers of human bronchial epithelial cells in the presence and absence of oligosaccharide inhibitors. Both encapsulated and nonencapsulated strains of S. pneumoniae grown to mid-logarithmic phase in suspension culture adhered to cultured primary respiratory epithelial cells and the conjunctival cell line. Adherence of nine clinically prevalent S. pneumoniae capsular types studied was inhibited preferentially by sialylated oligosaccharides that terminate with the disaccharide NeuAcalpha 2-3(or 6)Galbeta 1. Adherence of some strains also was weakly inhibited by oligosaccharides that terminate with lactosamine (Galbeta 1-4GlcNAcbeta 1). When sialylated oligosaccharides were covalently coupled to human serum albumin at a density of approximately 20 oligosaccharides per molecule of protein, the molar inhibitory potency of the oligosaccharide inhibitor was enhanced 500-fold. The above-mentioned experiments reveal a previously unreported dependence upon sialylated carbohydrate ligands for adherence of S. pneumoniae to human upper airway epithelial cells. Enhanced inhibitory potencies of polyvalent over monovalent forms of oligosaccharide inhibitors of adherence suggest that the putative adhesin(s) that recognizes the structure NeuAcalpha 2-3(or 6)Galbeta 1 is arranged on the bacterial surface in such a manner that it may be cross-linked by oligosaccharides covalently linked to human serum albumin.

* Corresponding author. Mailing address: Neose Technologies, 102 Witmer Rd., Horsham, PA 19044. Phone: (215) 773-1756. Fax: (215) 441-5896. E-mail: rbarthel{at}neose.com.




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Copyright © 1998 by the American Society for Microbiology. All rights reserved.