Neutral proteinase activities in different strains and clones of Entamoeba histolytica. Correlation with virulence.
Arch Med Res
; 23(2): 231-3, 1992.
Article
em En
| MEDLINE
| ID: mdl-1340301
ABSTRACT
Although several factors are involved in the invasive behavior of E. histolytica, proteinases seem to play a key role. Different proteinases have been found in virulent trophozoites of this parasite. Cytosols of clones A, 32-1 462-1 and L-6 of E. histolytica exhibiting various degrees of virulence were used to study the activity of trypsin-like, plasminogen activator and cathepsin B neutral proteinases with specific synthetic oligopeptides. Cathepsin-B like activity showed the highest values in highly virulent clone A, which is derived from virulent strain HM1IMSS. On the contrary, non virulent clones had very low activity. Clone L-6, a non virulent subclone of strain HM1IMSS, retained some cathepsin B-like activity. Trypsin-like and plasminogen activator assays revealed low activity and no differences between virulent and non-virulent clones were found. It is concluded that the Arg-Arg-thiol proteinase (Cathepsin B-like) is a good virulence marker.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Endopeptidases
/
Proteínas de Protozoários
/
Entamoeba histolytica
Limite:
Animals
Idioma:
En
Revista:
Arch Med Res
Assunto da revista:
MEDICINA
Ano de publicação:
1992
Tipo de documento:
Article