Neutralizing monoclonal antibody epitopes of the Entamoeba histolytica galactose adhesin map to the cysteine-rich extracellular domain of the 170-kilodalton subunit.

@article{Mann1993NeutralizingMA,
  title={Neutralizing monoclonal antibody epitopes of the Entamoeba histolytica galactose adhesin map to the cysteine-rich extracellular domain of the 170-kilodalton subunit.},
  author={Barbara J. Mann and Chee Yeun Chung and J. M. Dodson and L S Ashley and Laci Braga and Tomas Snodgrass},
  journal={Infection and immunity},
  year={1993},
  volume={61 5},
  pages={1772-8}
}
Entamoeba histolytica adheres to human colonic mucins and colonic epithelial cells via a galactose-binding adhesin. The adhesin is a heterodimeric glycoprotein composed of 170- and 35-kDa subunits. Fragments of the hgl1 gene encoding the 170-kDa subunit were expressed as recombinant fusion proteins in Escherichia coli and reacted with anti-adhesin monoclonal antibodies (MAbs) or pooled human immune sera. The MAbs tested recognize seven distinct epitopes on the 170-kDa subunit and have distinct… CONTINUE READING

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