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Updated: Aug 5, 2026

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
Published on: March 9, 2010
Immunological similarity between the 170 kD amoebic adherence glycoprotein and human beta 2 integrins
S A Adams1, S C Robson, V Gathiram
1University of Cape Town/Medical Research Council Liver Research Centre, Medical School, South Africa.
Abstract:
Amoebiasis is an important cause of morbidity and mortality in developing countries. Virulence of Entamoeba histolytica depends on the trophozoite's being able to bind to colonic epithelium; binding is mediated by the 170 kD subunit of a 260 kD lectin. We found, by microcytofluorometry and western blotting studies, that this 170 kD subunit protein shares an epitope with human beta 2 integrins--a subfamily of cell-surface glycoproteins expressed exclusively on leucocytes and involved in many adhesive and signalling interactions. The immunological similarity between these proteins may explain the trophozoite's ability to bind to and invade colonic epithelium.
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