Aspartic protease activities of schistosomes cleave mammalian hemoglobins in a host-specific manner
Mem. Inst. Oswaldo Cruz
;
102(1): 83-85, Feb. 2007. ilus
Artículo
en Inglés
| 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.
Texto completo:
Disponible
Índice:
LILACS (Américas)
Asunto principal:
Schistosoma japonicum
/
Schistosoma mansoni
/
Hemoglobinas
/
Ácido Aspártico Endopeptidasas
Límite:
Animales
/
Humanos
Idioma:
Inglés
Revista:
Mem. Inst. Oswaldo Cruz
Asunto de la revista:
Medicina Tropical
/
Parasitología
Año:
2007
Tipo del documento:
Artículo
País de afiliación:
Estados Unidos
Institución/País de afiliación:
Tulane University Health Sciences Center/US
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