Abstract
The 96-kDa surface antigen of Entamoeba histolytica was demonstrated through extensive immunologic evaluation with monoclonal and monospecific antibodies to be identical to or an isoform of the amebic alcohol/aldehyde dehydrogenase (EhADH2). EhADH2 was secreted, excreted, or shed into the culture medium in quantities commensurate with amebic growth when studied in a novel culture system. Of importance, using RNase protection assays, specific mRNA coding for the EhADH2 gene product(s) was up-regulated by treatment of viable trophozoites with the enzyme substrate ethanol. These data provide insight into the biology of this enzyme and its regulation by appropriate stressors.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Alcohol Dehydrogenase / immunology
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Alcohol Dehydrogenase / metabolism*
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Aldehyde Dehydrogenase / immunology
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Aldehyde Dehydrogenase / metabolism*
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Animals
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Antibodies, Monoclonal
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Antigens, Protozoan / immunology
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Antigens, Protozoan / metabolism*
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Antigens, Surface / immunology
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Antigens, Surface / metabolism
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Cross Reactions
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Culture Media
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Electrophoresis, Polyacrylamide Gel
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Entamoeba histolytica / drug effects
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Entamoeba histolytica / enzymology*
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Entamoeba histolytica / immunology
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Entamoeba histolytica / pathogenicity
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Ethanol / pharmacology
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Immunoblotting
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Isoenzymes / metabolism*
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Molecular Weight
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RNA, Messenger / metabolism
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Radioimmunoprecipitation Assay
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Up-Regulation
Substances
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Antibodies, Monoclonal
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Antigens, Protozoan
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Antigens, Surface
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Culture Media
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Isoenzymes
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RNA, Messenger
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Ethanol
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Alcohol Dehydrogenase
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Aldehyde Dehydrogenase