Schistosomiasis is a major health hazard in many regions of the world. Techniques for the diagnosis and treatment of this disease are not yet satisfactory.
The aims of this proposal are to isolate and purify specific enzymes of the adult worm of Schistosoma mansoni, to study their biochemical and immunological properties and to determine their utility in the diagnosis of schistosomiasis. These enzymes are acidic thiol-dependent proteinases, which may function in the nutrition of the worm, by digestion of host hemoglobin. These enzymes are regurgitated into the host's circulation, and we isolated two species of proteinases which lead to the production of antibodies in mice, baboons, and humans. The first objective of this proposal is to purify these proteinases to homogeneity and to determine their physical-chemical properties and structures by biochemical and immunological techniques. The second objective is to study the role of these proteinases in schistosome physiology and metabolism by determining the appearance of these enzymes during development, and to study their action on specific host blood proteins including hemoglobin and immunoglobins. The third objective is to obtain information about the structures of these enzymes using genetic and molecular cloning techniques.

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Unknown (R22)
Project #
5R22AI015864-08
Application #
3444503
Study Section
Tropical Medicine and Parasitology Study Section (TMP)
Project Start
1979-05-01
Project End
1991-02-28
Budget Start
1987-03-01
Budget End
1988-02-29
Support Year
8
Fiscal Year
1987
Total Cost
Indirect Cost
Name
Baylor College of Medicine
Department
Type
Schools of Medicine
DUNS #
074615394
City
Houston
State
TX
Country
United States
Zip Code
77030
Monroy, F P; Dresden, M H (1996) The developmental expression of cysteine proteinases in Schistosoma mansoni. Int J Parasitol 26:109-12
Yoshino, T P; Lodes, M J; Rege, A A et al. (1993) Proteinase activity in miracidia, transformation excretory-secretory products, and primary sporocysts of Schistosoma mansoni. J Parasitol 79:23-31
Rege, A A; Wang, W; Dresden, M H (1992) Cysteine proteinases from Schistosoma haematobium adult worms. J Parasitol 78:16-23
Chappell, C L; Dresden, M H; Gryseels, B et al. (1990) Antibody response to Schistosoma mansoni adult worm cysteine proteinases in infected individuals. Am J Trop Med Hyg 42:335-41
Chappell, C L; Hackel, J; Davis, A H (1989) Cloned Schistosoma mansoni proteinase (hemoglobinase) as a putative serodiagnostic reagent. J Clin Microbiol 27:196-8
Zerda, K S; Dresden, M H; Chappell, C L (1988) Schistosoma mansoni: expression and role of cysteine proteinases in developing schistosomula. Exp Parasitol 67:238-46
Chappell, C L; Kalter, D C; Dresden, M H (1988) The hypersensitivity response to the adult worm proteinase, SMw32, in Schistosoma mansoni infected mice. Am J Trop Med Hyg 39:463-8
Chappell, C L; Dresden, M H (1988) Antibody response to a purified parasite proteinase (SMw32) in Schistosoma mansoni infected mice. Am J Trop Med Hyg 39:66-73
Chappell, C L; Dresden, M H; Walters, D W (1987) Glutathione activation of a cysteine proteinase from Schistosoma mansoni. Biochim Biophys Acta 913:335-41
Chappell, C L; Dresden, M H (1987) Purification of cysteine proteinases from adult Schistosoma mansoni. Arch Biochem Biophys 256:560-8

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