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Infect Immun. 1997 December; 65(12): 5042–5051.
PMCID: PMC175727

A specific cell surface antigen of Streptococcus gordonii is associated with bacterial hemagglutination and adhesion to alpha2-3-linked sialic acid-containing receptors.


A Ca2+-independent lectin activity for alpha2-3-linked sialic acid-containing receptors is associated with Streptococcus gordonii DL1 (Challis) but not with a spontaneous mutant, strain D102, that specifically lacks hemagglutinating activity. Comparison of crossed-immunoelectrophoresis patterns of parent and mutant sonicated cell extracts identified a unique antigen (Hs antigen) in the parent cell extract that was purified by DEAE Sephacel column chromatography and by a wheat germ agglutinin (WGA) lectin affinity column. The purified antigen formed a single arc in crossed immunoelectrophoresis with anti-DL1 serum and migrated as a diffuse band above the 200-kDa marker in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Immunoelectron microscopy with specific anti-Hs antibody revealed labeling of structures in the fibrillar layer of strain DL1 and no labeling of fibrillar structures on strain D102. Rabbit anti-DL1 serum and anti-Hs Fab inhibited the hemagglutinating activity of strain DL1, and the inhibition was specifically neutralized by purified Hs antigen. Anti-Hs Fab did not inhibit the hemagglutinating activities of several heterologous S. gordonii strains; however, these bacteria were agglutinated by anti-Hs immunoglobulin G and also by WGA. In contrast, two S. gordonii strains that lacked hemagglutinating activity did not react with anti-Hs antibody or with WGA. These findings associate the sialic acid-binding lectin activity of S. gordonii DL1 with a specific fibrillar antigen, which is composed of protein and WGA reactive carbohydrate, and indicate that cross-reactive antigens occur on other strains of this species that possess hemagglutinating activity.

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Selected References

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  • Weeke B. A manual of quantitative immunoelectrophoresis. Methods and applications. 1. General remarks on principles, equipment, reagents and procedures. Scand J Immunol Suppl. 1973;1:15–35. [PubMed]
  • Bayer EA, Ben-Hur H, Wilchek M. Biocytin hydrazide--a selective label for sialic acids, galactose, and other sugars in glycoconjugates using avidin-biotin technology. Anal Biochem. 1988 May 1;170(2):271–281. [PubMed]
  • Cisar JO, Barsumian EL, Curl SH, Vatter AE, Sandberg AL, Siraganian RP. Detection and localization of a lectin on Actinomyces viscosus T14V by monoclonal antibodies. J Immunol. 1981 Oct;127(4):1318–1322. [PubMed]
  • Cisar JO, Kolenbrander PE, McIntire FC. Specificity of coaggregation reactions between human oral streptococci and strains of Actinomyces viscosus or Actinomyces naeslundii. Infect Immun. 1979 Jun;24(3):742–752. [PMC free article] [PubMed]
  • Clark WB, Wheeler TT, Cisar JO. Specific inhibition of adsorption of Actinomyces viscosus T14V to saliva-treated hydroxyapatite by antibody against type 1 fimbriae. Infect Immun. 1984 Feb;43(2):497–501. [PMC free article] [PubMed]
  • Demuth DR, Berthold P, Leboy PS, Golub EE, Davis CA, Malamud D. Saliva-mediated aggregation of Enterococcus faecalis transformed with a Streptococcus sanguis gene encoding the SSP-5 surface antigen. Infect Immun. 1989 May;57(5):1470–1475. [PMC free article] [PubMed]
  • Demuth DR, Davis CA, Corner AM, Lamont RJ, Leboy PS, Malamud D. Cloning and expression of a Streptococcus sanguis surface antigen that interacts with a human salivary agglutinin. Infect Immun. 1988 Sep;56(9):2484–2490. [PMC free article] [PubMed]
  • Demuth DR, Duan Y, Brooks W, Holmes AR, McNab R, Jenkinson HF. Tandem genes encode cell-surface polypeptides SspA and SspB which mediate adhesion of the oral bacterium Streptococcus gordonii to human and bacterial receptors. Mol Microbiol. 1996 Apr;20(2):403–413. [PubMed]
  • Demuth DR, Golub EE, Malamud D. Streptococcal-host interactions. Structural and functional analysis of a Streptococcus sanguis receptor for a human salivary glycoprotein. J Biol Chem. 1990 May 5;265(13):7120–7126. [PubMed]
  • Duan Y, Fisher E, Malamud D, Golub E, Demuth DR. Calcium-binding properties of SSP-5, the Streptococcus gordonii M5 receptor for salivary agglutinin. Infect Immun. 1994 Dec;62(12):5220–5226. [PMC free article] [PubMed]
  • Elder BL, Fives-Taylor P. Characterization of monoclonal antibodies specific for adhesion: isolation of an adhesin of Streptococcus sanguis FW213. Infect Immun. 1986 Nov;54(2):421–427. [PMC free article] [PubMed]
  • Fachon-Kalweit S, Elder BL, Fives-Taylor P. Antibodies that bind to fimbriae block adhesion of Streptococcus sanguis to saliva-coated hydroxyapatite. Infect Immun. 1985 Jun;48(3):617–624. [PMC free article] [PubMed]
  • Fairbanks G, Steck TL, Wallach DF. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971 Jun 22;10(13):2606–2617. [PubMed]
  • Fives-Taylor PM, Macrina FL, Pritchard TJ, Peene SS. Expression of Streptococcus sanguis antigens in Escherichia coli: cloning of a structural gene for adhesion fimbriae. Infect Immun. 1987 Jan;55(1):123–128. [PMC free article] [PubMed]
  • Ganeshkumar N, Arora N, Kolenbrander PE. Saliva-binding protein (SsaB) from Streptococcus sanguis 12 is a lipoprotein. J Bacteriol. 1993 Jan;175(2):572–574. [PMC free article] [PubMed]
  • Ganeshkumar N, Song M, McBride BC. Cloning of a Streptococcus sanguis adhesin which mediates binding to saliva-coated hydroxyapatite. Infect Immun. 1988 May;56(5):1150–1157. [PMC free article] [PubMed]
  • Gibbons RJ, Etherden I, Moreno EC. Association of neuraminidase-sensitive receptors and putative hydrophobic interactions with high-affinity binding sites for Streptococcus sanguis C5 in salivary pellicles. Infect Immun. 1983 Dec;42(3):1006–1012. [PMC free article] [PubMed]
  • Gibbons RJ, Etherden I, Moreno EC. Contribution of stereochemical interactions in the adhesion of Streptococcus sanguis C5 to experimental pellicles. J Dent Res. 1985 Feb;64(2):96–101. [PubMed]
  • Hawkes R. Identification of concanavalin A-binding proteins after sodium dodecyl sulfate--gel electrophoresis and protein blotting. Anal Biochem. 1982 Jun;123(1):143–146. [PubMed]
  • Hogg SD, Handley PS, Embery G. Surface fibrils may be responsible for the salivary glycoprotein-mediated aggregation of the oral bacterium Streptococcus sanguis. Arch Oral Biol. 1981;26(11):945–949. [PubMed]
  • Jenkinson HF, Demuth DR. Structure, function and immunogenicity of streptococcal antigen I/II polypeptides. Mol Microbiol. 1997 Jan;23(2):183–190. [PubMed]
  • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. [PubMed]
  • Levine MJ, Herzberg MC, Levine MS, Ellison SA, Stinson MW, Li HC, van Dyke T. Specificity of salivary-bacterial interactions: role of terminal sialic acid residues in the interaction of salivary glycoproteins with Streptococcus sanguis and Streptococcus mutans. Infect Immun. 1978 Jan;19(1):107–115. [PMC free article] [PubMed]
  • Lotan R, Sharon N, Mirelman D. Interaction of wheat-germ agglutinin with bacterial cells and cell-wall polymers. Eur J Biochem. 1975 Jun 16;55(1):257–262. [PubMed]
  • Maryanski JH, Wittenberger CL. Mannitol transport in Streptococcus mutans. J Bacteriol. 1975 Dec;124(3):1475–1481. [PMC free article] [PubMed]
  • McBride BC, Gisslow MT. Role of sialic acid in saliva-induced aggregation of Streptococcus sanguis. Infect Immun. 1977 Oct;18(1):35–40. [PMC free article] [PubMed]
  • McIntire FC, Crosby LK, Vatter AE. Inhibitors of coaggregation between Actinomyces viscosus T14V and Streptococcus sanguis 34: beta-galactosides, related sugars, and anionic amphipathic compounds. Infect Immun. 1982 Apr;36(1):371–378. [PMC free article] [PubMed]
  • McIntire FC, Vatter AE, Baros J, Arnold J. Mechanism of coaggregation between Actinomyces viscosus T14V and Streptococcus sanguis 34. Infect Immun. 1978 Sep;21(3):978–988. [PMC free article] [PubMed]
  • Misevic GN, Burger MM. Reconstitution of high cell binding affinity of a marine sponge aggregation factor by cross-linking of small low affinity fragments into a large polyvalent polymer. J Biol Chem. 1986 Feb 25;261(6):2853–2859. [PubMed]
  • Morris EJ, Ganeshkumar N, Song M, McBride BC. Identification and preliminary characterization of a Streptococcus sanguis fibrillar glycoprotein. J Bacteriol. 1987 Jan;169(1):164–171. [PMC free article] [PubMed]
  • Morris EJ, McBride BC. Adherence of Streptococcus sanguis to saliva-coated hydroxyapatite: evidence for two binding sites. Infect Immun. 1984 Feb;43(2):656–663. [PMC free article] [PubMed]
  • Murray PA, Levine MJ, Reddy MS, Tabak LA, Bergey EJ. Preparation of a sialic acid-binding protein from Streptococcus mitis KS32AR. Infect Immun. 1986 Aug;53(2):359–365. [PMC free article] [PubMed]
  • Murray PA, Levine MJ, Tabak LA, Reddy MS. Specificity of salivary-bacterial interactions: II. Evidence for a lectin on Streptococcus sanguis with specificity for a NeuAc alpha 2, 3Ga1 beta 1, 3Ga1NAc sequence. Biochem Biophys Res Commun. 1982 May 31;106(2):390–396. [PubMed]
  • Osterland CK, Miller EJ, Karakawa WW, Krause RM. Characteristics of streptococcal group-specific antibody isolated from hyperimmune rabbits. J Exp Med. 1966 Apr 1;123(4):599–614. [PMC free article] [PubMed]
  • PORTER RR. The hydrolysis of rabbit y-globulin and antibodies with crystalline papain. Biochem J. 1959 Sep;73:119–126. [PubMed]
  • Rosan B, Malamud D, Appelbaum B, Golub E. Characteristic differences between saliva-dependent aggregation and adhesion of streptococci. Infect Immun. 1982 Jan;35(1):86–90. [PMC free article] [PubMed]
  • Ruhl S, Sandberg AL, Cole MF, Cisar JO. Recognition of immunoglobulin A1 by oral actinomyces and streptococcal lectins. Infect Immun. 1996 Dec;64(12):5421–5424. [PMC free article] [PubMed]
  • Schneewind O, Fowler A, Faull KF. Structure of the cell wall anchor of surface proteins in Staphylococcus aureus. Science. 1995 Apr 7;268(5207):103–106. [PubMed]
  • Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. [PubMed]

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