Structural analysis and demonstration of the 29 kDa antigen of pathogenic Entamoeba histolytica as the major accessible free thiol-containing surface protein |
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| Authors: | Becky M Flores Mark A Batzer Murry A Stein Carolyn Petersen Dana L Diedrich Bruce E Torian |
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| Institution: | Department of Pharmaceutical Sciences, College of Pharmacy, Idaho State University, Pocatello, Indiana 83209-8334, USA.;Human Genome Center, Biomedical Sciences Division, L-452, Lawrence Livermore National Laboratory, P.O. Box 5507, Livermore, California 94551, USA.;Parasitology Laboratory, San Francisco General Hospital and the University of California San Francisco, San Francisco, California 94110, USA. |
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| Abstract: | The 29 kDa protein of pathogenic Entamoeba histolytica is a cysteine-rich surface antigen which we recently characterized by cDNA sequencing and by using monoclonal antibodies which differentiated between pathogenic and non-pathogenic clinical isolates. To determine the structure and biochemical attributes of this protein, a repertoire of immunologcal techniques using monoclonal antibodies, and radiolabelling were employed. We demonstrated that the 29 kDa protein forms a 60 kDa dimer and a high-molecular-mass oligomer(s) on the surface of the organism through disulphide bonds, and is the major accessible free thiol-containing surface protein of E. histolytica. The deduced amino acid sequence encoding the 29 kDa protein was found to share a common amino acid domain with sequences reported for Helicobacter pylori, Salmonella typhimurium, MER5 gene expressed in murine erythroleukemia cells, Clostridium pasteurianum, and a Bacillus spp. |
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