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Memórias do Instituto Oswaldo Cruz
Fundação Oswaldo Cruz, Fiocruz
ISSN: 1678-8060
EISSN: 1678-8060
Vol. 102, No. 1, 2007, pp. 83-85
Bioline Code: oc07014
Full paper language: English
Document type: Research Article
Document available free of charge

Memórias do Instituto Oswaldo Cruz, Vol. 102, No. 1, 2007, pp. 83-85

 en Aspartic protease activities of schistosomes cleave mammalian hemoglobins in a host-specific manner
Koehler, Jeffrey W; Morales, Maria E; Shelby, Bryan D & Brindley, Paul J

Abstract

We examined the efficiency of digestion of hemoglobin from four mammalian species, human, cow, sheep, and horse by acidic extracts of mixed sex adults of Schistosoma japonicum check for this species in other resources and S. mansoni. Activity ascribable to aspartic protease(s) from S. japonicum and S. mansoni cleaved human hemoglobin. In addition, aspartic protease activities from S. japonicum cleaved hemoglobin from bovine, sheep, and horse blood more efficiently than did the activity from extracts of S. mansoni. These findings support the hypothesis that substrate specificity of hemoglobin-degrading proteases employed by blood feeding helminth parasites influences parasite host species range; differences in amino acid sequences in key sites of the parasite proteases interact less or more efficiently with the hemoglobins of permissive or non-permissive hosts.

Keywords
schistosome - hemoglobin - aspartic protease - cathepsin D - host specificity - host range

 
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