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Molecular identity of a major antigen of Schistosoma mansoni which cross-reacts with Trichinella spiralis and Fasciola hepatica

Published online by Cambridge University Press:  06 April 2009

W. S. Aronstein ,
S. A. Lewis ,
A. P. Norden ,
J. P. Dalton  and
M. Strand
W. S. Aronstein
Affiliation:
Johns Hopkins University School of Medicine, Department of Pharmacology and Experimental Therapeutics, 725 North Wolfe Street, Baltimore, Maryland 21205, USA
S. A. Lewis
Affiliation:
Johns Hopkins University School of Medicine, Department of Pharmacology and Experimental Therapeutics, 725 North Wolfe Street, Baltimore, Maryland 21205, USA
A. P. Norden
Affiliation:
Johns Hopkins University School of Medicine, Department of Pharmacology and Experimental Therapeutics, 725 North Wolfe Street, Baltimore, Maryland 21205, USA
J. P. Dalton
Affiliation:
Johns Hopkins University School of Medicine, Department of Pharmacology and Experimental Therapeutics, 725 North Wolfe Street, Baltimore, Maryland 21205, USA
M. Strand
Affiliation:
Johns Hopkins University School of Medicine, Department of Pharmacology and Experimental Therapeutics, 725 North Wolfe Street, Baltimore, Maryland 21205, USA
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Summary

A glycoprotein cross-reactive among Schistosoma mansoni, Trichinella spiralis and Fasciola hepatica was identified and characterized by use of monoclonal antibodies prepared against S. mansoni glycoproteins. Four monoclonal antibodies recognized the same antigen which was one of the major S. mansoni glycoproteins precipitated by sera of hosts infected with either S. mansoni or T. spiralis. This antigen was expressed in S. mansoni cercariae, adult male and female worms, and eggs, and in S. haematobium but not in S. japonicum. Radio-immunoprecipitation and partial proteolytic digest mapping showed that the monoclonal antibodies each recognized a unique epitope. These epitopes were heat labile, sensitive to chaotropic agents, but resistant to reduction and alkylation or digestion with glycosidases, indicating that the recognition sites were amino acids and not carbohydrates. Epitopes recognized by the four monoclonal antibodies were expressed in F. hepatica, whereas only two were expressed in T. spiralis. Analysis by immunofluorescence microscopy showed that the antigen was expressed in S. mansoni in the parenchymal tissue and on the surface of the dorsal tubercles; in mature F. hepatica in the parenchymal tissue, vitelline glands and eggs; in immature F. hepatica only in the parenchymal tissue and in larval T. spiralis in the hypodermis.

Type
Research Article
Information
Parasitology , Volume 92 , Issue 1 , February 1986 , pp. 133 - 151
Copyright
Copyright © Cambridge University Press 1986

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References

REFERENCES

Abdel-Hafez, S. K., Phillips, S. M. & Zodda, D. M. (1983). Schistosoma mansoni: Detection and characterization of antigens and antigenemia by inhibition enzyme-linked immunosorbent assay (IELISA). Experimental Parasitology 55, 219–32.CrossRefGoogle ScholarPubMed
Anderson, R. I., Sadun, E. H. & Schoenbechler, M. J. (1963). Cross-absorption studies performed with Schistosoma mansoni and Trichinella, spiralis antigens in sera from patients with trichinosis. Experimental Parasitology 14, 323–9.CrossRefGoogle ScholarPubMed
Aronstein, W. S., Dalton, J. P. & Strand, M. (1985). A Schistosoma mansoni surface glycoprotein cross-reactive with a T1 antigen of Fasciola hepatica. American Journal of Tropical Medicine and Hygiene 34, 889–97.CrossRefGoogle ScholarPubMed
Aronstein, W. S., Dalton, J. P., Weiss, J. B. & Strand, M. (1985). Identification and characterization of a major Schistosoma mansoni glycoprotein antigen cross-reactive with Fasciola hepatica. American Journal of Tropical Medicine and Hygiene 34, 879–88.CrossRefGoogle Scholar
Aronstein, W. S. & Strand, M. (1983). Identification of species-specific and gender-specific proteins and glycoproteins of three human schistosomes. Journal of Parasitology 69, 1006–17.CrossRefGoogle ScholarPubMed
Barral-Netto, M., Hofstetter, M., Cheever, A. W. & Ottesen, E. A. (1983). Specificity of antibody and cellular immune responses in human schistosomiasis. American Journal of Tropical Medicine and Hygiene 32, 106–13.CrossRefGoogle ScholarPubMed
Boros, D. L., Tomford, R. & Warren, K. S. (1977). Induction of granulomatous and elicitation of cutaneous sensitivity by partially purified SEA of Schistosoma mansoni. Journal of Immunology 118, 373–6.CrossRefGoogle ScholarPubMed
Capron, A., Biguet, J., Vernes, A. & Afchain, D. (1968). Structure antigenique des helminthes. Aspects immunologiques des relations hote-parasite. Pathologie Biologie 16, 121–38.Google Scholar
Carter, C. E. & Colley, D. G. (1979). Partial purification and characterization of Schistosoma mansoni soluble egg antigen with Con A-Sepharose chromatography. Journal of Immunology 122, 2204–9.CrossRefGoogle ScholarPubMed
Carter, C. E. & Colley, D. G. (1981). Schistosoma japonicum soluble egg antigens: Separation by Con A chromatography and immunoaffinity purification. Molecular Immunology 18, 219–25.CrossRefGoogle ScholarPubMed
Cleveland, D. W., Fischer, S. G., Kirschner, M. W. & Laemmli, U. K. (1977). Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. Journal of Biological Chemistry 252, 1102–6.CrossRefGoogle ScholarPubMed
Diwan, A. R., Coker-Vann, M., Brown, P., Subianto, D. B., Yoken, R., Desowitz, R., Escobar, A., Gibbs, C. J. Jr. & Gajdusek, D. C. (1982). Enzyme-linked immunosorbent assay (ELISA) for the detection of antibody to cysticerci of Taenia solium. American Journal of Tropical Medicine and Hygiene 31, 364–9.CrossRefGoogle ScholarPubMed
Dresden, M. H. & Payne, D. C. (1981). A sieving method for the collection of schistosome eggs from mouse intestines. Journal of Parasitology 67, 450–2.CrossRefGoogle Scholar
Ey, P. L., Prowse, S. J. & Jenkin, C. R. (1978). Isolation of pure IgG1, IgG2a and IgG2b immuno globulins from mouse serum using protein A-sepharose. Immunochemistry 15, 429–36.CrossRefGoogle Scholar
Hanna, R. E. B. (1980). Fasciola hepatica: An immunofluorescent study of antigenic changes in the tegument during development in the rat and sheep. Experimental Parasitology 50, 155–70.CrossRefGoogle ScholarPubMed
Hanna, R. E. B. & Hillyer, G. V. (1984). Fasciola hepatica and Schistosoma mansoni: Immunofluor escence antigen localization and cross-reactivity. Experimental Parasitology 57, 1–14.CrossRefGoogle Scholar
Hillyer, G. V. (1984). Immunity to schistosomes using heterologous trematode antigens – a review. Veterinary Parasitology 14, 263–83.CrossRefGoogle ScholarPubMed
Hillyer, G. V. & Gomez De Rios, I. (1979). The enzyme-linked immunosorbent assay (ELISA) for the immunodiagnosis of schistosomiasis. American Journal of Tropical Medicine and Hygiene 28, 237–41.CrossRefGoogle ScholarPubMed
Hillyer, G. V., Ramzy, R. M. R., El Alamy, M. A. & Cline, B. L. (1981). The circumoval precipitin test for the serodiagnosis of human schistosomiasis mansoni and haematobia. American Journal of Tropical Medicine and Hygiene 30, 121–6.CrossRefGoogle ScholarPubMed
Huldt, G., Lagerquist, B., Phillips, T., Draper, C. C. & Voller, A. (1975). Detection of antibodies in schistosomiasis by enzyme-linked immunosorbent assay (ELISA). Annals of Tropical Medicine and Parasitology 69, 483–8.CrossRefGoogle Scholar
Hunter, W. M. (1967). The preparation of radioiodinated proteins of high activity, their reaction with antibody in vitro: the radioimmunoassay. In Handbook of Experimental Immunology (ed. Weir, D. M.), pp. 608–642. Philadelphia: F. A. Davis Co.Google Scholar
Jensenius, J. C. & Williams, A. F. (1974). The binding of anti-immunoglobulin antibodies to rat thymocytes and thoracic duct lymphocytes. European Journal of Immunology 4, 91–7.CrossRefGoogle ScholarPubMed
Kearney, J. F., Radbruch, A., Liesegang, B. & Rajewsky, K. (1979). A new mouse myeloma cell line that has lost immunoglobulin expression but permits the construction of antibody-secreting hybrid cell lines. Journal of Immunology 123, 1548–50.CrossRefGoogle ScholarPubMed
Köhler, G. & Milstein, C. (1975). Continuous cultures of fused cells secreting antibody of predefined specificity. Nature, London 256, 495–7.CrossRefGoogle ScholarPubMed
Köhler, G., Howe, S. E. & Milstein, C. (1976). Fusion between immunoglobulin-secreting and non-secreting myeloma cell lines. European Journal of Immunology 6, 292–5.CrossRefGoogle Scholar
Liu, C. & Bang, F. B. (1950). Agglutination of cercariae of Schistosoma mansoni by immune sera. Proceedings of the Society for Experimental Biology and Medicine 74, 68–72.CrossRefGoogle Scholar
Long, G. W., Lewert, R. M. & Pelley, R. P. (1981). Characterization of the glycoprotein antigens which mediate the Schistosoma japonicum circumoval precipitin reaction. Infection and Immunity 34, 389–96.CrossRefGoogle ScholarPubMed
Mariuzza, R. & Strand, M. (1981). Chemical basis for diversity in antibody specificity analyzed by hapten binding to monoclonal anti-4-hydroxy-3-nitrophenacetyl (NP) immunoglobulins. Molecular Immunology 18, 847–55.CrossRefGoogle Scholar
McLaren, M. L., Lillywhite, J. E., Dunne, D. W. & Doenhoff, M. J. (1981). Serodiagnosis of human Schistosoma mansoni infections: Enhanced sensitivity in ELISA using a fraction containing S. mansoni egg antigens w1 and #1. Transactions of the Royal Society Tropical Medicine and Hygiene 75, 72–9.CrossRefGoogle Scholar
Mitchell, G. F., Cruise, K. M., Garcia, E. G. & Anders, R. F. (1981). Hybridoma-derived antibody with immunodiagnostic potential for schistosomiasis japonica. Proceedings of the National Academy of Sciences, USA 78, 3165–9.CrossRefGoogle ScholarPubMed
Norden, A. P. (1984). Identification and characterization of immunogenic Schistosoma glycoproteins that are specific-specific, stage-specific, or react with sera from hosts infected with other parasites. Doctoral dissertation, The Johns Hopkins University, Baltimore, Maryland.Google Scholar
Norden, A. P., Aronstein, W. S. & Strand, M. (1982). Schistosoma mansoni: Identification, characterization, and purification of the spine glycoprotein by monoclonal antibody. Experimental Parasitology 54, 432–42.CrossRefGoogle ScholarPubMed
Norden, A. P. & Strand, M. (1984 a). Schistosoma mansoni, S. haematobium, and S. japonicum: Identification of genus-, species- and gender-specific antigenic worm glycoproteins. Experimental Parasitology 57, 110–23.CrossRefGoogle ScholarPubMed
Norden, A. P. & Strand, M. (1984 b). Schistosoma mansoni, S. haematobium, and S. japonicum: Identification of genus- and species-specific antigenic egg glycoproteins. Experimental Parasitology 58, 333–44.CrossRefGoogle ScholarPubMed
Norden, A. P. & Strand, M. (1985). Identification of antigenic Schistosoma mansoni glycoproteins during the course of infection in mice and humans. American Journal of Tropical Medicine and Hygiene 34, 495–507.CrossRefGoogle ScholarPubMed
Ogunba, E. O., Maddison, S. E., Tsang, V. C. W. & Slemenda, S. B. (1982). Reactivity of fractionated egg antigens of Schistosoma mansoni with sera of patients infected with S. haematobium. African Journal of Medical Science 11, 67–73.Google Scholar
Olivier, L. & Stirewalt, M. A. (1952). An efficient method for exposure of mice to cercariae of Schistosoma mansoni. Journal of Parasitology 38, 19–23.CrossRefGoogle ScholarPubMed
Pelley, R. P., Pelley, R. J., Hamburger, J., Peters, P. A. & Warren, K. S. (1976). Schistosoma mansoni soluble egg antigens. I. Identification and purification of three major antigens, and the employment of radioimmunoassay for their further characterization. Journal of Immunology 117, 1553–60.CrossRefGoogle ScholarPubMed
Rotmans, J. P. & Mooij, G. W. (1980). Separation and comparative immunoassay (DASS, ELISA) with antigens from adult Schistosoma mansoni. Transactions of the Royal Society for Tropical Medicine and Hygiene 74, 463–8.CrossRefGoogle ScholarPubMed
Sadun, E. H., Williams, J. S. & Anderson, R. I. (1960). Fluorescent antibody technic for serodiagnosis of schistosomiasis in humans. Proceedings of the Society for Experimental Biology and Medicine 105, 289–91.CrossRefGoogle ScholarPubMed
Salama, M. M. A., Aronstein, W. S., Weiss, J. B. & Strand, M. (1984). Monoclonal antibody identification of protein antigens in the liver of mice infected with Schistosoma mansoni. American Journal of Tropical Medicine and Hygiene 33, 608–20.CrossRefGoogle ScholarPubMed
Salih, S. Y., Bartlett, A. & Voller, A. (1978). Detection of antibodies by enzyme-immunoassay in human Schistosoma mansoni infections: A clinical and chemotherapeutic study. Tropenmedizin und Parasitologie 29, 409–12.Google ScholarPubMed
Schinski, V. D., Clutter, W. C. & Murrell, K. D. (1976). Enzyme- and 125I-labeled anti-immunoglobulin assays in the immunodiagnosis of schistosomiasis. American Journal of Tropical Medicine and Hygiene 25, 824–31.CrossRefGoogle ScholarPubMed
Slemenda, S. B., Hitchings, M. & Maddison, S. E. (1980). Standardization of FIAXTM for schistosomiasis using crude cercarial and adult worm antigens. Journal of Parasitology 66, 893–7.CrossRefGoogle ScholarPubMed
Strand, M. (1980). Transformation-related antigens identified by monoclonal antibodies. Proceedings of the National Academy of Sciences, USA 77, 3234–8.CrossRefGoogle ScholarPubMed
Strand, M., Aronstein, W. S., Norden, A. P., Lewis, S. A. & Weiss, J. B. (1984). Schistosoma worm proteins: Composition and immunoreactivity. In The Third John Jacob Abel Symposium on Molecular Parasitology (ed. August, J. T.), pp. 185–201. New York: Academic Press.Google Scholar
Strand, M., McMillan, A. & Pan, X. (1982). Schistosoma mansoni: Reactivity with infected human sera and monoclonal antibody characterization of a glycoprotein in different developmental stages. Experimental Parasitology 54, 145–56.CrossRefGoogle ScholarPubMed
Torpier, G., Capron, A. & Ouaissi, M. A. (1979). Receptor for IgG (Fc) and human beta 2-macroglobulin on S. mansoni schistosomula. Nature, London 278, 442–9.CrossRefGoogle Scholar
Tracy, J. W. & Mahmoud, A. A. F. (1982). Isolation of Schistosoma japonicium egg glycoprotein antigens which sensitize mice to lung granuloma formation and elicit and immediate hypersensitivity response. American Journal of Tropical Medicine and Hygiene 31, 1201–12.CrossRefGoogle Scholar
Tsang, V. C. W., Hancock, K., Kelly, M. A., Wilson, B. C. & Maddison, S. E. (1983). Schistosoma mansoni adult microsomal antigens, a serologic reagent. II. Specificity of antibody responses to the S. mansoni microsomal antigen (MAMA). Journal of Immunology 130, 1366–70.CrossRefGoogle Scholar
Tsang, V. C. W., Tao, Y. & Maddison, S. E. (1981). Systematic fractionation of Schistosoma mansoni urea-soluble egg antigens and their evaluation by the single-tube, kinetic-dependent, enzyme-linked, immonosorbent assay (K-ELISA). Journal of Parasitology 67, 340–50.CrossRefGoogle Scholar
Van Marck, E. A. E., Kestens, L., Stocker, S., Grimaud, J. A., Gigase, P. L. J. & Deelder, A. M. (1983). Fibrosis around schistosomal egg antigen-coated beads in the liver of mice. Contributions to Microbiology and Immunology 7, 251–9.Google ScholarPubMed
Yogure, M. G. Jr., Lewert, R. M. & Blas, B. L. (1981). Schistosomiasis japonica in Barrio San Antonio, Basey, Samar, in the Phillipines. American Journal of Tropical Medicine and Hygiene 30, 1252–62.Google Scholar