1887

Abstract

The polysaccharide (PS) located outside the peptidoglycan layer in ATCC 27092 was found to inhibit the adsorption of PL-1 phage to cell wall preparations without inactivating free phage. Electron microscopic examination of adsorption mixtures showed that the phage were adsorbed to fragments of PS material in a tail-first orientation. Phage did not adsorb to isolated peptidoglycan. The PS was composed of -rhamnose, -glucose, -glucosamine and -galactosamine, with the hexosamines possibly in -acetylated form. Prior treatment of with haemagglutinin, an anti-human blood group B agglutinin that binds specifically to -rhamnose, resulted in a concentration-dependent inhibition of phage adsorption. Phage adsorption was inhibited partially by lectins specific for -glucose and -acetyl--glucosamine, but not by lectins specific for -acetyl--glucosamine or -acetyl--galactosamine. The inhibition of phage adsorption occurred immediately upon the addition of the effective lectins, and was reversed by the addition of the respective lectin inhibitors, α-phenyl galactoside or α-methyl glucoside. The results indicate that -rhamnosyl residues are the main determinants of the PL-1 phage receptor sites, while -glucosyl residues may be involved more indirectly.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-128-10-2251
1982-10-01
2024-04-24
Loading full text...

Full text loading...

/deliver/fulltext/micro/128/10/mic-128-10-2251.html?itemId=/content/journal/micro/10.1099/00221287-128-10-2251&mimeType=html&fmt=ahah

References

  1. Ackerman H. W., Eisenstark A. 1974; The present state of phage taxonomy. Intervirology 3:201–209
    [Google Scholar]
  2. Archibald A. R., Coapes H. E. 1972; Blocking of bacteriophage receptors by concanavalin A. Journal of General Microbiology 73:581–585
    [Google Scholar]
  3. Birdsell D. C., Doyle R. J. 1973; Modification of bacteriophage ɸ25 adsorption to Bacillus subtilisby concanavalin A. Journal of Bacteriology 113:198–202
    [Google Scholar]
  4. Choy Y. M., Wong S. L., Lee C. Y. 1979; Change in surface carbohydrate-binding proteins of plants and animals. Carbohydrate Chemistry and Biochemistry 35:127–340
    [Google Scholar]
  5. Doyle R. J., Birdsell D. C. 1972; Interaction of concanavalin A with the cell wall of Bacillus subtilis. Journal of Bacteriology 109:652–658
    [Google Scholar]
  6. Entlicher G., KoŠtiŘ J. V., Kocaurek J. 1970; Studies on phytohemagglutinins. III. Isolation and characterization of hemagglutinins from the PEA. Biochimica et biophysica acta 221:272–281
    [Google Scholar]
  7. Fujita Y., Oishi K., Aida K. 1973; Sugar specificity of anti-B hemagglutinin produced by Streptomyces sp. Biochemical and Biophysical Research Communications 53:495–501
    [Google Scholar]
  8. Fujita Y., Oism K., Suzuki K., Imahori K. 1975; Purification and properties and an anti-B hemagglutinin produced by Streptomyces sp. Biochemistry 14:4465–4470
    [Google Scholar]
  9. Goldstein I. J., Hayes C. E. 1978; The lectins: carbohydrate-binding proteins of plants and animals. Advances in Carbohydrate Chemistry and Biochemistry 35:127–340
    [Google Scholar]
  10. Goldstein I. J., Iyer R. N. 1966; Interaction of concanavalin A, a phytohemagglutinin, with model substrates. Biochimica et biophysicaacta 121:197–200
    [Google Scholar]
  11. Goldstein I. J., Misaki A. 1970; Interaction of concanavalin A with an arabinolactan from the cell wall of Mycobacterium bovis. Journal of Bacteriology 103:422–425
    [Google Scholar]
  12. Goldstein I. J., Staub A. M. 1970; Interaction of concanavalin A with polysaccharides of Salmonella. Immunochemistry 17:315–319
    [Google Scholar]
  13. Gould N. R., Scheinberg S. L. 1970; Isolation and partial characterization of two anti-A hemagglutinins from P. lunatus. Archives of Biochemistry and Biophysics 137:1–11
    [Google Scholar]
  14. Hamada S., Gill K., Slade H. D. 1977; Binding of lectins to Streptococcus mutans cells and type-specific polysaccharides, and the effect on adherence. Infection and Immunity 18:708–716
    [Google Scholar]
  15. Hammarstr6M S., Rabat E. A. 1969; Purification and characterization of a blood-group A reactive hemagglutinin from the snail Helix pomatia and a study of its combining site. Biochemistry 8:2696–2705
    [Google Scholar]
  16. Howard I. K., Sage H. J. 1969; Isolation and characterization of a phytohemagglutinin from the lentil. Biochemistry 8:2436–2441
    [Google Scholar]
  17. Irimura T., Osawa T. 1972; Studies on a hemagglutinin from Bauhinia purpureaalba seeds. Archives of Biochemistry and Biophysics 151:475–482
    [Google Scholar]
  18. Liener I. E. 1958; Inactivation studies on the soybean hemagglutinin. Journal of Biological Chemistry 233:401–405
    [Google Scholar]
  19. Liener I. E. 1976; Isolation and properties of concanavalin A. In Concanavalin A as Tool pp. 17–31 Bittiger H., Schneble H. P. Edited by London:: John Wiley.;
    [Google Scholar]
  20. Nagata Y., Burger M. M. 1972; Wheat germ agglutinin.Isolation and crystallization. Journal of Biological Chemistry 247:2248–2250
    [Google Scholar]
  21. Nicolson G., Blaustein J. 1972; The interaction of Ricinus communis agglutinin with normal and tumor cell surfaces. Biochmica et biophysica acta 266:543–547
    [Google Scholar]
  22. Osawa T. 1975; Lectins (in Japanese). Kagaku To Seibutsu 13:273–280
    [Google Scholar]
  23. Osawa T., Akiya S. 1961; Immunochemical studies on blood-group specificity. I. Partial purification and properties of plant agglutinin (lectin) of Sophora japonica. Bulletin of Tokyo Medical and Dental University 8:287–298
    [Google Scholar]
  24. Picken R. N., Beacham I. R. 1977; Bacteriophage-resistant mutants of Escherichia coli K12 with altered lipopolysaccharide.Studies with con- canavalin A. Journal of General Microbiology 102:319–326
    [Google Scholar]
  25. Reeder W. J., Ekstedt R. D. 1971; Study of the interaction of concanavalin A with Staphylococcolteichoic acids. Journal of Immunology 106:334–340
    [Google Scholar]
  26. Robbins J. H. 1964; Tissue culture studies of the human lymphocyte. Science 146:1648–1654
    [Google Scholar]
  27. Sharon N., Lis H. 1972; Lectins: cell-agglutinating and sugar-specific proteins. Science 177:949–959
    [Google Scholar]
  28. Sumner J. B., Howell S. F. 1936; The identification of the hemagglutinin of the jack bean with concanavalin A. Journal of Bacteriology 32:227–237
    [Google Scholar]
  29. Toyoshima S., Akiyama Y., Nakano K., Tonomura A., Osawa T. 1971; A phytomitogen from Wisteria floribunda seeds and its interaction with human peripheral lymphocytes. Biochemistry 10:4457–4463
    [Google Scholar]
  30. Watanabe T., Shiomi T. 1976; Effect of plant lectins on λ-phage receptor sites of Bacillus anthracis. Japanese Journal of Microbiology 20:147–149
    [Google Scholar]
  31. Watanabe K., Takesue S. 1975; Use of l-rhamnose to study irreversible adsorption of bacteriophage PL-1 to a strain of Lactobacillus casei. Journal of General Virology 28:29–35
    [Google Scholar]
  32. Watanabe K., Takesue S., Jin-Nai K., Yoshikawa T. 1970; Bacteriophage active against the lactic acid beverage-producing bacterium, Lactobacillus casei. Applied Microbiology 20:409–415
    [Google Scholar]
  33. Watanabe K., Takesue S., Ishibashi K. 1977; Reversibility of the adsorption of bacteriophage PL-1 to the cell walls isolated from Lactobacillus casei. Journal of General Virology 34:189–194
    [Google Scholar]
  34. Watanabe K., Takesue S., Ishibashi K. 1980; Electron microscopic studies on the interaction between Lactobacillus phage PL-1 and cell walls isolated from its host cells. Journal of General and Applied Microbiology 26:413–420
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-128-10-2251
Loading
/content/journal/micro/10.1099/00221287-128-10-2251
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error