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Selective lectin reactions of two stocks of Leishmania enriettii with differing pathogenicity

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Abstract

Five days old promastigote culture forms of two stocks of Leishmania enriettii pathogenic and non-infective for Cavia procellus, were tested with the lectins of Canavalia ensiformis, Ricinus communis-120, Soja hispida (Glycine maxima), Arachis hypogaea, Ulex europaeus, Ulex europaeus I, Ulex europaeus II, Laburnum alpinum, Lotus tetragonolobus, Euonymus europaeus and with a monoclonal antibody against blood group H. The pathogenic stock reacted with the anti-H lectin of Lotus tetragonolobus and the monoclonal anti-H and the monoclonal anti-H but not with anti-H of U. europaeus I and E. europaeus. The non-infective stock reacted with none of these anti-H specific agglutinins. They had strong agglutination reactions to C. ensiformis (500 Μg/ml, 1,000 Μg/ml, 10 mg/ml) R. communis-120 (1∶10), S. hispida (1,000 Μg/ml) and A. hypogaea (500 Μg/ml, 1,000 Μg/ml, 2,000 Μg/ml). They showed moderate agglutinations to U. europaeus, L. alpinum and U. europaeus II. The non-infective stock showed only moderate reactions to C. ensiformis (10 mg/ml), R. communis-120 (1∶10), A. hypogaea (2,000 Μg/ml) and S. hispida (1,000 Μg/ml). Neither N-acetylneuraminic acid nor neuraminidase was detected on the cell surface of both stocks. This result demonstrates clearly that both stocks of L. enriettii differ in their cell surface carbohydrates. The agglutination reactions with lectins of the non-infective stock of L. enriettii are very similar to L.t. major.

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References

  • Adler S (1963) Differentiation of Leishmania braziliensis from L. mexicana and L. tropica. Rev Inst Salubr Enferm Trop (Mex) 23:139–150

    Google Scholar 

  • Alves RJR, Colli W (1974) Agglutination of Trypanosoma cruzi by concanavalin. A J Protozool 21:575–578

    Google Scholar 

  • Aminoff D (1961) Methods for the quantitative estimation of neurominic acid and their application to hydrolysates of sialomucoids. Biochem J 81:384–392

    Google Scholar 

  • Bencomo W, Sinay P (1983) Synthesis of glycopeptides having clusters of O-glycosylic disaccharide chains (Β-D-Gal-)1-3)-α-D-GalNAc) located at vicinal amino acid residues of the peptide chain. Carbohydr Res 116:C9-C12

    Google Scholar 

  • Bittinger H, Schnebli HP (1976) Concanavalin A as a Tool. John Wiley and Sons, London, New York, Sydney, Toronto

    Google Scholar 

  • BØg-Hansen TC (1981) Lectin-Biology, Biochemistry, Clinical Biochemistry, vol 1. Walter de Gruypter, Berlin New York

    Google Scholar 

  • BØg-Hansen TC (1982) Lectin-Biology, Biochemistry, Clinical Biochemistry, vol 2. Walter de Gruypter, Berlin New York

    Google Scholar 

  • BØg-Hansen TC (1983) Lectin-Biology, Biochemistry, Clinical Biochemistry, vol 3. Walter de Gruypter, Berlin New York

    Google Scholar 

  • Cohen E (1974) Biomedical Perspectives of agglutinins of invertebrate and plant origin. Ann NY Acad Sci, vol 234

  • Dawidowicz K, Hernandez AG, Infante RB (1975) The surface membrane of Leishmania. I. The effects of lectins on different stages of Leishmania braziliensis. J Parasitol 61:950–953

    Google Scholar 

  • Gold ER, Balding P (1975) Receptor-specific-proteins. Ex Medica Amsterdam

  • Goldstein IJ, Hayes CE (1978) The lectins: Carbohydrate binding proteins of plant and animals. Adv Carbohydr Chem Biochem 35:127–340

    Google Scholar 

  • Hakomori SI (1971) Glycolipid changes associated with malignant transformation. In: Hölzl Wallach DF, Fischer M (eds) The dynamic structures of cell membranes. Springer, Berlin Heidelberg New York

    Google Scholar 

  • Holthöfer H, Virtanen I, Kariniemi L, Hormia M, Lindner E, Miettinen A (1982) Ulex europaeus I lectin as a marker for vascular endothelium in human tissues. Lab Invest 47:60–66

    Google Scholar 

  • Hoover RL (1974) Surface characterization of two Amoebae relative to cell adhesion. Exp Cell Res 87:265–276

    Google Scholar 

  • Krüpe M (1970) Die Blutgruppen des Menschen — Eine übersicht, Selbstverlag Fulda

  • Luther P (1982) Lektin and Toxin der Mistel. Academie, Berlin

    Google Scholar 

  • Martinez-Palomo A, Gonzalez-Robles A, Torre de la M (1973) Selective agglutination of pathogenic strains of Entamoeba histolytica induced Con A. Nature New Biol 245:186–187

    Google Scholar 

  • Matsumoto I, Osawa T (1969) Purification and characterization of an anti-H(O) phytohemagglutinin of Ulex europaeus. Biochim Biophys Acta 194:180

    Google Scholar 

  • Matsumoto T, Osawa T (1971) On the specificity of various heterologous anti-H hemagglutinins. Vox Sang 21:548

    Google Scholar 

  • Menezes H (1971) Applicacao de vacina viva avirulenta de Trypanosoma cruzi emseres humanos. Rev Inst Med Trop Sao Paulo 13:144–154

    Google Scholar 

  • Müller HE (1974) Neuraminidases of mycoplasma, bacteria and protozoa — neuraminidases of bacteria and protozoa and their pathogenic role. Behring Inst Mitt 55:34–56

    Google Scholar 

  • Muniz J, Medina H (1948) Leishmaniose tegumentar do cobaio, Leishmania enriettii nsp “O Hospital”, Rio de Janeiro XXXIII 1:7–25

    Google Scholar 

  • Nicolson GL (1974) The interaction of lectins with animal surfaces. Int Rev Cytol 39:90–190

    Google Scholar 

  • Nicolson GL (1976) Transmembrane control of the receptors on normal and tumor cells. Biochim Biophys Acta 457:57–108

    Google Scholar 

  • Oppenheim JY, Rosenstreich DL (1976) Mitogens in immunology. Acad Press, New York San Francisco London

    Google Scholar 

  • Pereira MEA, Kabat EA (1974) Specificity of purified hemagglutinin (Lectin) from Lotus tetragonolobus. Biochemistry 13:3184–3192

    Google Scholar 

  • Pereira MEA, Kisailus EC, Gruezo F, Kabat EA (1978) Immunochemical studies on the combining site of the blood group H specific lectin 1 from Ulex europaeus seeds. Arch Biochem Biophys 185:108–115

    Google Scholar 

  • Petryniak J, Goldstein IJ (1984) Comparative immunochemical studies on L-fucose-binding lectins. In: Vliegenthardt JFG, Kamerling JP, Veldink GA (eds) Abstracts of the XII the International Carbohydrate Symposium, Utrecht, Netherlands. Von Publishers, P2G2

    Google Scholar 

  • Petryniak J, Dus D, Podwinska J (1983) Agglutination of murine and guinea pig peritoneal cells by L-fucose binding lectin: Evonymus europaeus. Eur Immunol 13:459–464

    Google Scholar 

  • Prokop O, Uhlenbruck G (1966) Lehrbuch der menschlichen Blut- und Serumgruppen. VEB Georg Thieme, Leipzig

    Google Scholar 

  • Roth J (1978) The lectins-molecular probes in cell biology and membrane research. VEB Gustav Fischer, Jena

    Google Scholar 

  • Schottelius J (1982) Lectin binding strain specific carbohydrates on the cell surfaces of leishmania strains from the old world. Z Parasitenkd 66:237–247

    Google Scholar 

  • Schottelius J (1986) Thiobarbituric acid/methylumbelliferyl test for the differentiation of Trypanosoma cruzi and Trypanosoma rangeli. Zentralbl Bakteriol (in press)

  • Schottelius J, Da Costa SC Goncalves (1982) Studies on the relationship between lectin binding carbohydrates and different strains of Leishmania from the new world. Mem Inst Oswaldo Cruz, Rio de Janeiro 77:19–27

    Google Scholar 

  • Sharon N (1975) Blood group substances. In: Complex carbohydrates, p 227 Addison-Wesley Publ Comp, London, Amsterdam. Don Mill, Ontario, Sydney, Tokyo

    Google Scholar 

  • Stevens AR, Kaufman AE (1974) Concanavalin A induced agglutination of Acanthamoeba. Nature 252:43–45

    Google Scholar 

  • Uhlenbruck G (1971) Immunbiologie. Wilhelm Goldmann, München

    Google Scholar 

  • Vischer P, Reutter W (1978) Specific alterations of fucoprotein biosynthesis in the Plasma Membrane of Morris Hepatoma 7777. Eur J Biochem 84:363–368

    Google Scholar 

  • Warton A, Honigberg BM (1980) Lectin analysis of surface saccharides in two Trichomonas vaginalis strains differing in pathogenicity. J Protozool 27:410–419

    Google Scholar 

Download references

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Supported in the context of a Research Programme of the Commission of the European Communities and the Bernhard-Nocht-Institute for Nautical and Tropical Medicine, Department of Protozoology, Hamburg, TSD-005-D(B)

The work was supported by the Ministry for Youth, Family Affairs and Health

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Schottelius, J. Selective lectin reactions of two stocks of Leishmania enriettii with differing pathogenicity. Parasitol Res 73, 1–8 (1987). https://doi.org/10.1007/BF00536329

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