1887

Abstract

Surmmary

Some plate-grown strains of that were harvested into phosphate-buffered saline and left for 1 h released soluble haemagglutinins. These caused high-titre agglutination of human and guinea-pig erythrocytes, whereas chicken, sheep and bovine erythrocytes were agglutinated at various titres. Six of 10 strains which had been subcultured repeatedly did not possess soluble haemagglutinins. Slide agglutination of bacterial suspensions demarcated the strains into two groups; Group 1 gave strong agglutination with most types of erythrocyte, Group 2 did not. By microtitration assay, all Group-1 strains but only two Group-2 strains produced a soluble haemagglutinin. Cell-associated haemagglutinins were found by microtitration assay in all strains of , but higher titres were found within Group-1 strains. The supernates of broth-grown, shaken cultures also showed the presence of soluble haemagglutinins, with higher titres for recently isolated strains. Pre-treatment of human erythrocytes with neuraminidase from and abolished haemagglutination by the soluble, but not by the cell-associated haemagglutinin. The soluble haemagglutinin was inhibited by sialoproteins containing predominantly the N-acetylneuraminyl (2–3) galactopyranosyl [NeuAc(2–3)Gal] structure, fetuin, glycophorin and bovine N-acetylneuraminyl-lactose (NeuAc-Lac). Transferrin and human NeuAc-Lac, which contain predominantly the N-acetylneuraminyl (2–6) galactopyranosyl [NeuAc(2–6)Gal] structure were not inhibitory. However, bovine submaxillary mucin (BSM) was strongly inhibitory; it contains several structures with sialic acid linked 2–6 to oligosaccharides. These results suggest that the soluble haemagglutinin recognises a NeuAc(2–3)Gal structure, but has high affinity for another, as yet undetermined, sialic acid-containing structure.

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1990-12-01
2022-01-17
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References

  1. Goodwin CS. Duodenal ulcer, Campylobacter pylori, and the “leaking roof’ concept. Lancet 1988; 2:1467–1469
    [Google Scholar]
  2. Graham DY. Campylobacter pylori and peptic ulcer disease. Gastroenterology 1989; 96:615–625
    [Google Scholar]
  3. Romaniuk PJ, Zoltowaska B, Trust TJ. et al. Campylobacter pylori, the spiral bacterium associated with human gastritis, is not a true Campylobacter sp. J Bacteriol 1987; 169:2137–2141
    [Google Scholar]
  4. Goodwin CS, Armstrong JA, Chilvers T. et al. Transfer of Campylobacter pylori and Campylobacter mustelae to Helicobacter gen. nov. as Helicobacter pylori comb. nov. and Helicobacter mustelae comb. nov. respectively. Int J Syst Bacteriol 1989; 39:397–405
    [Google Scholar]
  5. Klemm P. Fimbrial adhesins of Escherichia coli. Rev Infect Dis 1985; 7:321–340
    [Google Scholar]
  6. Hanne LF, Finkelstein RA. Characterization and distribu tion of the hemagglutinins produced by Vibrio cholerae. Infect Immun 1982; 36:209–214
    [Google Scholar]
  7. Freter R, Jones GW. Models for studying the role of bacterial attachment in virulence. Rev Infect Dis 1983; 5: Suppl 4S647–S658
    [Google Scholar]
  8. Evans DG, Evans DJ, Moulds JJ, Graham DY. N- acetylneuraminyllactose-binding fibrillar hemagglutinin of Campylobacter pylori: a putative colonization factor antigen. Infect Immun 1988; 56:2896–2906
    [Google Scholar]
  9. Huang J, Smyth CJ, Kennedy NP, Arbuthnott JP, Keeling PWN. Haemagglutinating activity of Campylobacter pylori. FEMS Microbiol Lett 1988; 56:109–112
    [Google Scholar]
  10. Emödy L, Carlsson Å, Ljungh Å, Wadström T. Mannose-resistant haemagglutination by Campylobacter pylori. Scand J Infect Dis 1988; 20:353–354
    [Google Scholar]
  11. Nakazawa T, Ishibashi M, Konishi H, Takemoto T, Shigeeda M, Kochiyima T. Hemagglutination activity of Campylobacter pylori. Infect Immun 1989; 57:989–991
    [Google Scholar]
  12. Leunk RD, Ferguson MA, Morgan DR. In-vitro adherence and hemagglutination by Campylobacter pylori . In Ruiz-Palacios GM. (ed) Campylobacter V. Proceedings of the fifth international workshop on Campylobacter infections. Mexico: 1989 in press
    [Google Scholar]
  13. Goodwin CS, Blincow ED, Warren JR, Waters TE, Sanderson CR, Easton L. Evaluation of cultural techniques for isolating Campylobacter pyloridis from endoscopic biopsies of gastric mucosa. J Clin Pathol 1985; 38:1127–1131
    [Google Scholar]
  14. Armstrong JA, Wee SH, Goodwin CS, Wilson DH. Response of Campylobacter pyloridis to antibiotics, bismuth and an acid-reducing agent in vitro—an ultrastructural study. J Med Microbiol 1987; 24:343–350
    [Google Scholar]
  15. Gunnarson A, Märdh P-A, Lundblad A, Svensson S. Oligosaccharide structures mediating agglutination of sheep erythrocytes by Staphylococcus saprophyticus. Infect Immun 1984; 45:41–46
    [Google Scholar]
  16. Paul RW, Lee PWK. Glycophorin is the reovirus receptor on human erythrocytes. Virology 1987; 159:94–101
    [Google Scholar]
  17. Angel MA, Bumess ATH. The attachment of encephalo- myocarditis virus to erythrocytes from several animal species. Virology 1977; 83:428–432
    [Google Scholar]
  18. Eylar EH, Madoff MA, Brody OV, Oncley JL. The contribution of sialic acid to the surface charge of the erythrocyte. J Biol Chem 1962; 237:1992–2000
    [Google Scholar]
  19. Shukla AK, Schauer R. Fluorimetric determination of unsubstituted and 9(8)-O-acetylated sialic acids in erythrocyte membranes. Hoppe-Seyler’s Z Physiol Chem 1982; 363:255–262
    [Google Scholar]
  20. Sarris AH, Palade GE. The sialoglycoproteins of murine erythrocyte ghosts. J Biol Chem 1979; 254:6724–6731
    [Google Scholar]
  21. Tsuji T, Osawa T. Carbohydrate structures of bovine submaxillary mucin. Carbohydr Res 1986; 151:391–402
    [Google Scholar]
  22. Lingwood CA, Law H, Pellizzari A, Sherman P, Drumm B. Gastric glycerolipid as a receptor for Campylobacter pylori. Lancet 1989; 2:238–241
    [Google Scholar]
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