Aspartic protease activities of schistosomes cleave mammalian hemoglobins in a host-specific manner
Mem. Inst. Oswaldo Cruz
;
102(1): 83-85, Feb. 2007. ilus
Article
in English
| LILACS
| ID: lil-440638
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 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.
Full text:
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Index:
LILACS (Americas)
Main subject:
Schistosoma japonicum
/
Schistosoma mansoni
/
Hemoglobins
/
Aspartic Acid Endopeptidases
Limits:
Animals
/
Humans
Language:
English
Journal:
Mem. Inst. Oswaldo Cruz
Journal subject:
Tropical Medicine
/
Parasitology
Year:
2007
Type:
Article
Affiliation country:
United States
Institution/Affiliation country:
Tulane University Health Sciences Center/US
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