Monoclonal antibodies directed against the galactose-binding lectin of Entamoeba histolytica enhance adherence.

@article{Petri1990MonoclonalAD,
  title={Monoclonal antibodies directed against the galactose-binding lectin of Entamoeba histolytica enhance adherence.},
  author={William A Petri and Tomas Snodgrass and Terry F H G Jackson and V Gathiram and Ahmed E Simjee and Kris Chadee and Martin D. Chapman},
  journal={Journal of immunology},
  year={1990},
  volume={144 12},
  pages={4803-9}
}
The Entamoeba histolytica galactose-binding lectin is a surface glycoprotein composed of 170- and 35-kDa subunits. Inhibition of this lectin with galactose or anti-170 kDa subunit polyclonal antibody blocks amebic adherence to target cells and colonic mucin glycoproteins. We describe the properties of 10 mAb with specificity for the 170-kDa subunit. Based on competitive binding studies, six nonoverlapping antigenic determinants on the lectin were identified. The effect of the mAb on adherence… CONTINUE READING
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