The glutathione transferase activity and tissue distribution of a cloned Mr28K protective antigen of Schistosoma mansoni

• Published in: The EMBO journal 1988-02, Vol.7 (2), p.465-472
• Main Authors: Taylor, J. B., Vidal, A., Torpier, G., Meyer, D. J., Roitsch, C., Balloul, J. M., Southan, C., Sondermeyer, P., Pemble, S., Lecocq, J. P.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Antigens, Helminth - genetics; Antigens, Helminth - immunology; Biological and medical sciences; Biotechnology; Cloning, Molecular; Cross Reactions; Escherichia coli - genetics; Fundamental and applied biological sciences. Psychology; Genetic engineering; Genetic technics; Glutathione Transferase - genetics; Glutathione Transferase - immunology; Glutathione Transferase - metabolism; Humans; Macromolecular Substances; Methods. Procedures. Technologies; Microscopy, Electron; Molecular cloning; Molecular Sequence Data; Molecular Weight; Saccharomyces cerevisiae - genetics; Schistosoma mansoni - enzymology; Schistosoma mansoni - genetics; Schistosoma mansoni - ultrastructure
• ISSN: 0261-4189; 1460-2075
• DOI: 10.1002/j.1460-2075.1988.tb02834.x

A protective Mr28K antigen of Schistosoma mansoni, expressed from its cDNA, has been purified in a single step and shown to possess glutathione (GSH) transferase activity as predicted from sequence homologies with two mammalian GSH transferase multigene families. It is notable for its high 1‐chloro‐2,4‐dinitrobenzene GSH transferase and linoleic acid hydroperoxide GSH peroxidase activities. The major GSH transferase of S. mansoni has been purified and its subunit is identical to this Mr28K antigen by criteria of Mr, immunochemistry, substrate specificity and peptide sequence analysis. In the parasite, the antigen is present in the tegument, protonephridial cells and subtegumental parenchymal cells. No significant immunological cross‐reactivity between the S.mansoni and mammalian (human and rat) GSH transferases was observed.