[Interaction of the cytoskeleton of E. histolytica with human erythrocytes]

The mechanism by which trophozoites of E histolytica destroy mammalian cells has been correlated with the polymerization of the actin contained in the amoeba's cytoskeleton. This is preceded by the attachment of the amoeba lectins with carbohydrates in the cell surface. Here we describe the events of the interaction of E histolytica cytoskeleton with human red blood cells using fluorescence microscopy of glutaraldehyde-fixed trophozoites membrane removed with triton X-100 and stained with rhodamine-phalloidin. The challenge with RBC revealed a maximum polymerization two minutes after the challenge. The most active phagocytosis was observed four minutes after challenge. The use of fluorescent phalloidin showed to be a fast method which specifically binds to the F form of actin; this method is easier than methods which use monoclonal antibodies to identify actin.