1887

Abstract

Summary

The ability of 25 lectins, isolated from different plants and fungi, to agglutinate 95 clinical isolates of β-haemolytic streptococci was examined. Cell suspensions were untreated, trypsin-treated or boiled at pH 2.0. None of the 95 untreated cell suspensions gave a visible reaction with any of the lectins. When the cells were trypsinised, 42 strains were agglutinated with one or more lectin and after boiling at pH 2, all the strains were agglutinated. After treatment with trypsin, 20 different agglutination patterns were observed, and after boiling, 19 patterns, four of which were similar. A correlation was found between Lancefield group C and some of these patterns. Some lectins reacted specifically with group C streptococci; DBA and WFA, both specific for D-Ga1NAc, DSA, a G1cNAc-specific lectin, and RPA, which showed a complex specificity, reacted only with group C strains. Furthermore, the lectin of reacted with 50% of group B streptococci only. Agglutination assays with lectins were reproducible, easy to perform, relatively inexpensive and, therefore, applicable to studies of cell-wall structure and epidemiology of β-haemolytic streptococci.

Loading

Article metrics loading...

/content/journal/jmm/10.1099/00222615-39-6-440
1993-12-01
2024-12-03
Loading full text...

Full text loading...

/deliver/fulltext/jmm/39/6/medmicro-39-6-440.html?itemId=/content/journal/jmm/10.1099/00222615-39-6-440&mimeType=html&fmt=ahah

References

  1. Goldstein IJ, Hughes RC, Monsigny M, Osawa T, Sharon N. What should be called a lectin?. Nature 1980; 285:66
    [Google Scholar]
  2. Damjanov I. Biology of disease. Lectin cytochemistry and histochemistry. Lab Invest 1987; 57:5–20
    [Google Scholar]
  3. Pistole TG. Interaction of bacteria and fungi with lectins and lectin-like substances. Annu Rev Microbiol 1981; 35:85–112
    [Google Scholar]
  4. Kohler W, Prokop O, Kuhnemund O. Routine identification of group-C streptococci by means of an agglutinin (protectin) from the albumen gland of the edible snail, Helix pomatia. J Med Microbiol 1973; 6:127–130
    [Google Scholar]
  5. Ottensooser F, Nakamizo Y, Sato M, Miyamoto Y, Takizawa K. Lectins detecting group C streptococci. Infect Immun 1974; 9:971–973
    [Google Scholar]
  6. Wagner M. Agglutination of bacteria by a sialic acid-specific lectin of the snail Cepaea hortensis. Acta Histochem 1982; 71:35–39
    [Google Scholar]
  7. Slifkin M, Cumbie R. Identification of group B streptococcal antigen with lectin-bound polystyrene particles. J Clin Microbiol 1987; 25:1172–1175
    [Google Scholar]
  8. Aitchison EJ, Lambert PA, Farrell ID. Antigenic composition of an endocarditis-associated isolate of Streptococcus faecalis and identification of its glycoprotein antigens by ligand blotting with lectins. J Med Microbiol 1986; 21:161–167
    [Google Scholar]
  9. Slifkin M, Doyle RJ. Lectins and their application to clinical microbiology. Clin Microbiol Rev 1990; 3:197–218
    [Google Scholar]
  10. O’Sullivan N, Benjamin J, Skirrow MB. Lectin typing of Campylobacter isolates. J Clin Pathol 1990; 43:957–960
    [Google Scholar]
  11. Moyes A, Young H. An analysis of lectin agglutination as a means of sub-dividing gonococcal serovars. J Med Microbiol 1992; 37:51–55
    [Google Scholar]
  12. Jarlov JO, Hansen J-ES, Rosdahl VT, Espersen F. The typing of Staphylococcus epidermidis by a lectin-binding assay. J Med Microbiol 1992; 37:195–200
    [Google Scholar]
  13. Lotan R, Skutelsky E, Danon D, Sharon N. The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea). J Biol Chem 1975; 250:8518–8523
    [Google Scholar]
  14. Peumans WJ, Nsimba-Lubaki M, Peeters B, Broekaert WF. Isolation and partial characterization of a lectin from ground elder (Aegopodium podagraria) rhizomes. Planta 1985; 164:75–82
    [Google Scholar]
  15. Van Damme EJM, Goldstein IJ, Peumans WJ. A comparative study of related mannose-binding lectins from Amaryl-lidaceae and Alliaceae species. Phytochemistry 1991; 30:509–514
    [Google Scholar]
  16. Peumans WJ, Nsimba-Lubaki M, Carlier AM, Van Driessche E. A lectin from Bryonia dioica root stocks. Planta 1984; 160:222–228
    [Google Scholar]
  17. Broekaert WF, Peumans WJ, Allen AK. Carbohydrate binding proteins from Datura stramonium seeds. In: Bog-Hansen TC, Breborowicz J. (eds) Lectins, vol 4 Berlin, New York: Walter de Gruyter Co.; 1985481–489
    [Google Scholar]
  18. Kawaguchi T, Matsumoto I, Osawa T. Studies on hemag glutinins from Maackia amurensis seeds. J Biol Chem 1974; 249:2786–2792
    [Google Scholar]
  19. Wantyghem J, Goulut C, Frenoy J-P, Turpin E, Goussault Y. Purification and characterization of Robinia pseudoacacia seed lectins. A re-investigation. Biochem J 1986; 237:483–489
    [Google Scholar]
  20. Kellens JTC, Peumans WJ. Occurrence of lectins in different strains of Rhizoctonia solani. In: Kocourek J, Freed DJL. (eds) Lectins, vol. 7 St Louis: Sigma Chemical Co.; 199057–62
    [Google Scholar]
  21. Kellens JTC, Goldstein IJ, Peumans WJ. Lectins in different members of the Sclerotiniaceae. My col Res 1992; 96:495–502
    [Google Scholar]
  22. Kaku H, Peumans WJ, Goldstein IJ. Isolation and characterization of a second lectin (SNA-II) present in elderberry (Sambucus nigra L.) bark. Arch Biochem Biophys 1990; 111:255–262
    [Google Scholar]
  23. Cammue BPA, Peeters B, Peumans WJ. A new lectin from tulip (Tulipa) bulbs. Planta 1986; 169:583–588
    [Google Scholar]
  24. Kurokawa T, Tsuda M, Sugino Y. Purification and characterization of a lectin from Wisteria floribunda seeds. J Biol Chem 1976; 251:5686–5693
    [Google Scholar]
  25. Nagata Y, Burger MM. Wheat germ agglutinin. Molecular characteristics and specificity for sugar binding. J Biol Chem 1974; 249:3116–3122
    [Google Scholar]
  26. Agrawal BBL, Goldstein IJ. Protein-carbohydrate interaction. VI. Isolation of concanavalin A by specific adsorption on cross-linked dextran gels. Biochim Biophys Acta 1967; 147:262–271
    [Google Scholar]
  27. Etzler ME, Kabat EA. Purification and characterization of a lectin (plant hemagglutinin) with blood group A specificity from Dolichos biflorus. Biochemistry 1970; 9:869–877
    [Google Scholar]
  28. Ziska P, Franz H, Kindt A. The lectin from Viscum album L. purification by biospecific affinity chromatography. Experientia 1978; 34:123–124
    [Google Scholar]
  29. Wagner M. Interaction of wheat-germ agglutinin with streptococci and streptococcal cell wall polymers. Immunobiology 1979; 156:57–64
    [Google Scholar]
  30. Knibbs RN, Goldstein IJ, Ratcliffe RM, Shibuya N. Characterization of the carbohydrate binding specificity of the leukoagglutinating lectin from Maackia amurensis. J BiolChem 1991; 266:83–88
    [Google Scholar]
  31. Shibuya N, Goldstein IJ, Broekaert WF, Nsimba-Lubaki M, Peeters B, Peumans WJ. The elderberry (Sambucus nigra L.) bark lectin recognizes the Neu5Ac(a2-6)GalNAc sequence. J Biol Chem 1987; 262:1596–1601
    [Google Scholar]
  32. Lim DV, Morales WJ, Walsh AF, Kazanis D. Reduction of morbidity and mortality rates for neonatal group B streptococcal disease through early diagnosis and chemoprophylaxis. J Clin Microbiol 1986; 23:489–492
    [Google Scholar]
/content/journal/jmm/10.1099/00222615-39-6-440
Loading
/content/journal/jmm/10.1099/00222615-39-6-440
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