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At least 181 records · Page 10Linked to original sources
PubMed1978

Promitosis and rod occurrence in the limax ameba Vahlkampfia lobospinosa.

Nuclear division and trophozoite structure and function were investigated in Vahlkampfia lobospinosa. During karyokinesis the nucleolus remained present and divided to form polar masses. Chromatids separated and were directed to the polar masses by spindle fibers within an intact nuclear membrane. No interzonal body was formed. Trophozoites consistently contained and extruded a rod-like structure 10-15 X 1-2 micron. Although it was found in other areas of the cell within the cytoplasm, this rod most frequently protruded from the uroid.

Amoeba↗
PubMed1992

Effects of magainins on ameba and cyst stages of Acanthamoeba polyphaga.

Amebic keratitis produced by Acanthamoeba spp. is an increasingly important ocular infection in extended-use contact lens wearers. Problems associated with the infection are compounded by the lack of effective and well-tolerated chemotherapeutic agents. The magainins, a group of naturally occurring and synthetic membrane-active peptide compounds, have been shown to be active in vitro against a clinical isolate of Acanthamoeba polyphaga. Two magainins tested extensively had minimal inhibitory and minimal amebicidal values of 20 and 25 micrograms/ml for magainin MSI-103 and 25 and 40 micrograms/ml for magainin MSI-94, respectively. Both amebastatic and amebicidal activities are enhanced by combining the magainins with silver nitrate (200 micrograms/ml) and/or other marginally effective antimicrobial agents. These combinations have activity against both trophic and cystic stages in the Acanthamoeba life cycle and have promise as antimicrobial agents in the treatment of amebic keratitis.

Acanthamoeba↗
PubMed1994

Human secretory immunoglobulin A anti-Entamoeba histolytica antibodies inhibit adherence of amebae to MDCK cells.

The presence of secretory immunoglobulin A (IgA) anti-Entamoeba histolytica antibodies in the saliva of patients with intestinal amebiasis was demonstrated by immunoblot assay, and the capacity of these antibodies to inhibit amebic adherence to a monolayer of MDCK cells was analyzed. Inhibition was due to IgA antiamebic antibodies and in part to anti-Gal-binding-lectin antibodies, as demonstrated by absorption experiments with total amebic extract and with the fraction of Gal-binding lectin. These results emphasize the relevance of secretory IgA antibodies in the phenomenon of E. histolytica adherence to epithelial cells.

Animals↗