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Purification of an agglutinin from the haemolymph of the snail Bulinus nasutus and demonstration of related proteins in other Bulinus spp.

Published online by Cambridge University Press:  06 April 2009

R. A. Harris ,
T. M. Preston  and
V. R. Southgate
R. A. Harris
Affiliation:
Department of Biology, Medawar Building, University College London, Gower Street, London WC 1E 6BT
T. M. Preston*
Affiliation:
Department of Biology, Medawar Building, University College London, Gower Street, London WC 1E 6BT
V. R. Southgate
Affiliation:
Experimental Taxonomy Division, The Natural History Museum, Cromwell Road, London SW7 5BD
*
†Dr T. M. Preston, Department of Biology, Medawar Building, University College London, Gower Street, London WC1E 6BT
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Summary

The snail Bulinus nasutus 1214 possesses a potent haemagglutinin (end-point titre with human erythrocytes, 2−18) in its cell-free haemolymph which also binds to the miracidia (but not other larvae) of the incompatible parasite Schistosoma margrebowiei. We have purified a protein possessing this haemagglutinating property from the plasma of this snail. The native Mr of this protein was estimated by SDS polyacrylamide gel electrophoresis to be 210 kDa; under denaturing conditions in a 7.5% PAGE gel it ran as a major band of 135 kDa. Proteins of similar Mr were also found in the haemolymph of 16 other Bulinus spp. (the major intermediate hosts of human and veterinary schistosomiasis in Africa) although the plasma of none of these agglutinated human erythrocytes. Nonetheless, Cleveland mapping of the Mr 135 kDa bands from these different Bulinus spp. revealed 4 identical major peptide fragments (30, 28, 19 and 16 kDa) in each, thus demonstrating a similarity in the primary structure of these plasma proteins. Antisera from Balb/C mice immunized with the 135 kDa polypeptide from Bulinus truncatus 1521 cross-reacted in Western blots with the 135 kDa band of other members of the same truncatus/tropicus species complex but not with species from the africanus or forskalii species groups.

Keywords

Bulinushaemagglutininhaemolymph proteinSchistosomaintermediate host resistance
Type
Research Article
Information
Parasitology , Volume 106 , Issue 2 , February 1993 , pp. 127 - 135
Copyright
Copyright © Cambridge University Press 1993

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References

REFERENCES

Afonso, A. M. M., Arrieta, M. R. & Neves, A. G. A. (1976). Characterization of the haemoglobin of Biomphalaria glabrata as a glycoprotein. Biochimica et Biophysica Acta 439, 77–81.CrossRefGoogle ScholarPubMed
Bayne, C. J., Buckley, P. M. & DeWan, P. (1980). Schistosoma mansoni: cytotoxicity of haemocytes from susceptible snail hosts from sporocysts in plasma from resistant Biomphalaria glabrata. Experimental Parasitology 50, 409–16.CrossRefGoogle Scholar
Boswell, C. A. & Bayne, C. J. (1984). Isolation, characterization and functional assessment of a haemagglutinin from the plasma of Biomphalaria glabrata, intermediate host of Schistosoma mansoni. Developmental and Comparative Immunology 8, 559–68.CrossRefGoogle ScholarPubMed
Daniel, B. E., Preston, T. M. & Southgate, V. R. (1992). The in vitro transformation of the miracidium to the mother sporocyst of Schistosoma margrebowiei; changes in the parasite surface and implications for interactions with snail plasma factors. Parasitology 104, 41–9.CrossRefGoogle Scholar
Granath, W. O., Spray, F. J. & Judd, R. C. (1987). Analysis of Biomphalaria glabrata (Gastropoda) haemolymph by SDS-PAGE, HPLC, and immunoblotting. Journal of Invertebrate Pathology 49, 198–208.CrossRefGoogle ScholarPubMed
Hammarström, S., Westöö, A. & Björk, J. (1972). Subunit structure of Helix pomatia A haemagglutinin. Scandinavian journal of Immunology 1, 295–309.CrossRefGoogle Scholar
Harris, R. A. (1990). Haemolymph proteins and the snail immune response. Ph.D. thesis. University of London.Google Scholar
Jeong, K. H., Sussman, S., Rosen, S. D., Lie, K. J. & Heyneman, D. (1981). Distribution and variation of haemagglutinating activity in the haemolymph of Biomphalaria glabrata. journal of Invertebrate Pathology 28, 256–63.CrossRefGoogle Scholar
Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, London 27, 680–5.CrossRefGoogle Scholar
Michelson, E. H. & Dubois, L. (1977). Agglutinins and lysins in the family Planorbidae: a survey of haemolymph, egg masses, and albumen gland extracts. Biological Bulletin 153, 219–27.CrossRefGoogle ScholarPubMed
Morrissey, J. H. (1981). Silverstain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity. Analytical Biochemistry 117, 307–10.CrossRefGoogle Scholar
Renwrantz, L. & Berliner, U. (1978). A galactose specific agglutinin, a blood-group H active polysaccharide, and a trypsin inhibitor in albumin glands and eggs of Arianta arbustorum (Helicidae). Journal of Invertebrate Pathology 31, 171–9.CrossRefGoogle Scholar
Renwrantz, L. & Stahmer, A. (1983). Opsonizing properties of an isolated hemolymph agglutinin and demonstration of lectin-like recognition molecules at the surface of hemocytes from Mytilus edulis. Journal of Comparative Physiology 149, 535–46.CrossRefGoogle Scholar
Sarkar, M., Bachhauwat, B. K. & Mandal, C. (1984). A new cold agglutinin from Achatina fulica snails. Archives of Biochemistry and Biophysics 233, 286–9.CrossRefGoogle ScholarPubMed
Uhlenbruck, G. & Prokop, O. (1966). An agglutinin from Helix pomatia which reacts with terminal N-acetyl-D- galactosamine. Vox Sanguinis 11, 519–26.Google ScholarPubMed
van der Knaap, w. P. w. & Loker, E. S. (1990). Immune mechanisms in trematode–snail interactions. Parasitology Today 6, 175–82.CrossRefGoogle ScholarPubMed
van der Knaap, W. P. W., Doderer, A., Boerrigter-Barendsen, L. H. & Sminia, T. (1982). Some properties of an agglutinin in the haemolymph of the pond snail Lymnaea stagnalis. Biological Bulletin 162, 404–12.CrossRefGoogle Scholar
Wagner, M. (1982). Agglutination of bacteria by a sialic acid-specific lectin of the snail Cepea hortensis. Acta Histochemica 71, 35–9.CrossRefGoogle Scholar
Yoshino, T. P. & Bayne, C. J. (1983). Mimicry of snail host antigens by miracidia and primary sporocysts of Schistosoma mansoni. Parasite Immunology 5, 317–28.CrossRefGoogle ScholarPubMed
Yoshino, T. P., Cheng, T. C. & Renwrantz, L. R. (1977). Lectin and human blood group determinants of Schistosoma mansoni: alteration following in vitro transformation of miracidium to mother sporocysts. Journal of Parasitology 63, 818–24.CrossRefGoogle Scholar
Zelck, U. & Becker, W. (1990). Lectin binding to cells of Schistosoma mansoni sporocysts and surrounding Biomphalaria glabrata tissue. Journal of Invertebrate Pathology 55, 93–9.CrossRefGoogle ScholarPubMed