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

Becky M. Flores, Samuel L. Stanley, Tai Soon Yong, Manzoor Ali, Wengang Yang, Dana L. Diedrich, Bruce E. Torian

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)226-231
Number of pages6
JournalJournal of Infectious Diseases
Volume173
Issue number1
DOIs
Publication statusPublished - 1996

Bibliographical note

Funding Information:
Received 12 July 1995; revised 30 August 1995. Financial support: National Institutes of Health (AI-28188 to B.E.T.; AI-37977 and AI-01231 [Public Health Service Career Development Award] to S.L.S.); Monsanto Company (to S.L.S.). Reprints or correspondence: Dr. Bruce E. Torian, Idaho State University, College of Pharmacy, Dept. of Pharmaceutical Sciences, 970 S. 5th Ave., Pocatello, ID 83209-8334.

All Science Journal Classification (ASJC) codes

  • Immunology and Allergy
  • Infectious Diseases

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