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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

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