Hostname: page-component-78c5997874-8bhkd Total loading time: 0 Render date: 2024-11-14T04:28:58.477Z Has data issue: false hasContentIssue false

Proteoglycans from adult worms of Schistosoma haematobium

Published online by Cambridge University Press:  05 June 2009

R.R. Hamed
Affiliation:
Molecular Biology Department, National Research Center, Dokki, Cairo, Egypt:
T.M. Maharem
Affiliation:
Biochemistry Department, Faculty of Science, Ain Shams University, Cairo, Egypt
A.S. El-Guindy
Affiliation:
Molecular Biology Department, National Research Center, Dokki, Cairo, Egypt:

Abstract

Different types of proteoglycans (PGs) from adult worms of Schistosoma haematobium, were sequentially extracted using chaotropic agents under associative conditions (0.5 M GnCl), dissociative conditions (4 M GnCl) and detergents (Triton X-100 and SDS). The extracts were designated Fl, F2, F3 and F4, respectively. The highest amount of uronic acid and carbohydrate was detected in the associative extract (Fl) while the highest amount of protein was detected in the SDS extract (F4). Agarose polyacrylamide gel electrophoresis (A-PAGE) indicated the presence of a different PG in each extract with different electrophoretic mobilities. Agarose gel electrophoresis of glycosaminoglycan (GAG) separated from GnCl, associative and dissociative extracts, and the residue suggested the presence of dermatan sulphate in the two extracts and the residue, in addition to a GAG-like material found in the associative extract only. This glycosaminoglycan showed resistance to digestion with all mucopolysaccharidases and nitrous acid treatment. Gel filtration chromatography of associative extract on Sepharose CL-6B indicated the presence of three main uronic acid peaks (P1, P2 and P3). Chondroitin sulphate was the main GAG that could be detected in peak one (P1). Peak two (P2) contains carbohydrate and uronic acid but has no protein or absorbance at 280 nm. P2 has two types of GAGs: dermatan sulphate and a GAG-like material. The role of this PG in helping the adult schistosomes in evading immobilization by the host blood clotting cascade is discussed. Antibodies to peak one and peak two were detected in hamster sera infected with S. haematobium and S. mansoni using the ELISA test. The specificity of peak two was found to be evident in its low cross-reactivity (18.9%) when confronted with S. mansoni infected sera.

Type
Research Papers
Copyright
Copyright © Cambridge University Press 1997

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Albano, R.M. & Mourano, P.A.S. (1983) Presence of sulfated glycans in ascidian tunic and in the body wall of sea cucumber. Biochimica et Biophysica Acta 760, 192196.CrossRefGoogle Scholar
Andreani, D.D. & Gray, C.H. (1956) Serum polysaccharide in diabetes mellitus. Clinica Chimica Acta 1, 715.CrossRefGoogle ScholarPubMed
Bergwerf, A.A., Van Dam, G.J., Rotmans, J.P., Deelder, A.M., Kamerling, J.P. & Vliegenthart, J.F.G. (1994) The immunologically reactive part of immunopurified circulating anodic antigen from Schistosoma mansoni is a threonine-linked polysaccharide consisting of →6)-(β-D-glcpA-(1→3))-β-D-GalpNAc-(1→repeating units. Journal of Biological Chemistry 269, 3151031517.CrossRefGoogle Scholar
Bitter, T. & Muir, H.M. (1962) A modified uronic carbazole reaction. Analytical Biochemistry 4, 330334.CrossRefGoogle ScholarPubMed
Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72, 248254.CrossRefGoogle ScholarPubMed
Carney, S.L. (1986) Proteoglycans. pp. 97141in Chapplin, M.F. & Kennedy, J.F. (Eds) Carbohydrate analysis. Oxford, Washington DC, IRL Press.Google Scholar
Cassaro, C.M. & Dietrich, C.P. (1977) Distribution of sulfated mucopolysaccharides in invertebrates. Journal of Biological Chemistry 252, 22542261.CrossRefGoogle ScholarPubMed
Cooper, N.R. (1985) The classical complement pathway activation and regulation of the first complement component. Advances in Immunology 37, 151216.CrossRefGoogle ScholarPubMed
Damle, S.P., Kieras, F.J., Tzeng, W. & Gregory, J.D. (1979) Isolation and characterization of proteochondroitin sulfate from pig skin. Journal of Biological Chemistry 254, 16141620.CrossRefGoogle ScholarPubMed
Dunne, D.W. (1990) Schistosome carbohydrates. Parasitology Today 6 (2), 4548.CrossRefGoogle ScholarPubMed
Engvall, E. & Berlman, P. (1971) Enzyme-linked immunosorbent assay (ELISA). Quantitative assay of immunoglobulin-G. Immunochemistry 8, 781784.CrossRefGoogle ScholarPubMed
Gowda, D.C., Bhavanandon, V.P. & Davidson, E.A. (1986) Isolation and characterization of proteoglycans secreted by normal and malignant human mammary cells. Journal of Biological Chemistry 261, 49264934.CrossRefGoogle Scholar
Hockley, D.J. & McLaren, D.J. (1973) Schistosoma mansoni: Changes in the outer membrane of the tegument during development from cercariae to adult worms. International Journal for Parasitology 3, 1325.CrossRefGoogle Scholar
Hook, M., Kjellen, L., Johansson, S. & Robinson, J. (1984) Cell surface glycosaminoglycans. Annual Revieiv of Biochemistry 53, 847869.CrossRefGoogle ScholarPubMed
Horton, D. & Philips, K.D. (1973) Nitrous acid deamintion of glycosides and acetates of 2-amino-2- deoxy-D-glucose. Carbohydrate Research 30, 367374.CrossRefGoogle Scholar
Jackson, R.L., Busch, S.J. & Cardin, A.D. (1991) Glycosaminoglycans: molecular properties, protein interactions, and role in physiological processes. Physiological Reviews 71, 481539.CrossRefGoogle ScholarPubMed
Kelly, C., Payares, G., Simpson, A.J.G. & Smithers, S.R. (1987) Surface and species-specific antigens of S. haematobium. Parasitology 95, 253266.CrossRefGoogle Scholar
Kjellen, L. & Lindahl, U. (1991) Proteoglycans: Structures and interactions. Annual Review of Biochemistry 60, 443475.CrossRefGoogle ScholarPubMed
Kojima, T., Cataldo, W.L., Marchildon, G.A., Marcum, J.A. & Rosenberg, R.D. (1992) Isolation and characterization of heparan sulfate proteoglycans produced by the cloned rat microvascular endothelial cells. Journal of Biological Chemistry 267, 48594869.CrossRefGoogle ScholarPubMed
Lagunoff, D. & Warren, G. (1962) Determination of 2-deoxy-2-sulfamatoaminohexose content of mucopolysacchrides. Archives of Biochemistry and Biophysics 99, 396403.CrossRefGoogle Scholar
McDevitt, C.A. & Muir, H. (1971) Gel electrophoresis of proteoglycans and glycosaminoglycans on large pore composite polyacrylamide-agarose gels. Analytical Biochemistry 44, 612622.CrossRefGoogle ScholarPubMed
Nash, T.E., Prescott, B. & Neva, F.A. (1974) The characteristics of a circulating antigen. Journal of Immunology 112, 15001508.CrossRefGoogle ScholarPubMed
Nash, T.E., Nasir-Ud-Din, & Jeanloz, R.W. (1977) Further purification and characterization of circulating antigen in schistosomiasis. Journal of Immunology 119, 16271634.CrossRefGoogle ScholarPubMed
Omer-Ali, P., Smithers, S.R., Bickle, Q., Philips, S.M., Horn, D. & Simpson, A.J.G. (1988) Analysis of the anti-Schistosoma mansoni surface antibody response during murine infection and its contribution to protective immunity. Journal of Immunology 140, 32733279.CrossRefGoogle ScholarPubMed
Poole, A.R., Webber, C., Reiner, A. & Roughley, P.J. (1989) Studies of monoclonal antibody to skeletal keratan sulfate. Biochemical Journal 260, 849856.CrossRefGoogle Scholar
Robertson, N.P. & Cain, G.D. (1985) Isolation and characterization of glycosaminoglycans from S. mansoni. Comparative Biochemistry and Physiology 82, 299306.Google Scholar
Robertson, N.P., Oaks, J.A. & Cain, G.D. (1984) Biochemical characterization of polysaccharides of the eggs and adults of Hymenolepis diminuta. Molecular and Biochemical Parasitology 10, 99109.CrossRefGoogle Scholar
Simpson, A.J.G., Correa-Oliveira, R., Smithers, S.R. & Sher, A. (1983) The exposed carbohydrates of schistosomula of Schistosoma mansoni and their modification during maturation in vivo. Molecular and Biochemical Parasitology 8, 191205.CrossRefGoogle ScholarPubMed
Tsang, V.C.W., Hubbard, W.J. & Damian, R.T. (1977) Coagulation factor XIIa (activated Hageman Factor) inhibitor from adult S. mansoni. American Journal of Tropical Medicine and Hygiene 26, 243247.CrossRefGoogle Scholar
Van Dam, G.J., Seino, J., Rotman, J.P., Daha, M.R. & Deelder, A.M. (1993) Schistosoma mansoni circulating anoding antigen but not circulatory cathoding antigen interacts with complement C1q. European Immunology 23, 28072812.CrossRefGoogle ScholarPubMed