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
Dans Anglais
| 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.
Texte intégral:
Disponible
Indice:
LILAS (Amériques)
Sujet Principal:
Schistosoma japonicum
/
Schistosoma mansoni
/
Hémoglobines
/
Aspartic acid endopeptidases
Limites du sujet:
Animaux
/
Humains
langue:
Anglais
Texte intégral:
Mem. Inst. Oswaldo Cruz
Thème du journal:
Médecine tropicale
/
Parasitologie
Année:
2007
Type:
Article
Pays d'affiliation:
États-Unis d'Amérique
Institution/Pays d'affiliation:
Tulane University Health Sciences Center/US
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