Literature DB >> 8537663

Surface localization, regulation, and biologic properties of the 96-kDa alcohol/aldehyde dehydrogenase (EhADH2) of pathogenic Entamoeba histolytica.

B M Flores1, S L Stanley, T S Yong, M Ali, W Yang, D L Diedrich, B E Torian.   

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.

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Year:  1996        PMID: 8537663     DOI: 10.1093/infdis/173.1.226

Source DB:  PubMed          Journal:  J Infect Dis        ISSN: 0022-1899            Impact factor:   5.226


  2 in total

1.  Complementation of an Escherichia coli adhE mutant by the Entamoeba histolytica EhADH2 gene provides a method for the identification of new antiamebic drugs.

Authors:  T S Yong; E Li; D Clark; S L Stanley
Journal:  Proc Natl Acad Sci U S A       Date:  1996-06-25       Impact factor: 11.205

Review 2.  Progress towards development of a vaccine for amebiasis.

Authors:  S L Stanley
Journal:  Clin Microbiol Rev       Date:  1997-10       Impact factor: 26.132

  2 in total

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