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Neutral proteinase activities in different strains and clones of Entamoeba histolytica. Correlation with virulence.

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 HM1:IMSS. On the contrary, non virulent clones had very low activity. Clone L-6, a non virulent subclone of strain HM1:IMSS, 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.