Use of monoclonal anti-light subunit antibodies to study the structure and function of theEntamoeba histolytica Gal/GalNAc adherence lectin |
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Authors: | James J. McCoy Alissa M. Weaver William A. Petri Jr |
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Affiliation: | (1) From the Departments of Medicine, Microbiology and Pathology, University of Virginia School of Medicine, 22908 Charlottesville, VA, USA;(2) University of Virginia Health Sciences Center, Room 2115 MR4 Building, 22908 Charlottesville, VA, USA |
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Abstract: | Adherence ofEntamoeba histolytiea trophozoites to host cells is medicated by a galactose (Gal) andN-acetylgalactosamine (GalNAc)-specific surface lectin. The lectin is a heterodimeric protein composed of heavy (170kDa) and light (35-31 kDa) subunits linked by disulfide bonds. Polyclonal and monoclonal antibodies (mAb) raised against a light subunit-glutathione-S-transferase fusion protein were used to probe its structure and function. Four light subunit-specific mAb were produced which recognized distinct epitopes on five different light subunit isoforms. Immunoblots with these mAb demonstrated co-migration of light and heavy subunits when nonreduced trophozoite proteins were analysed by SDS-PAGE, indicating that the subunits do not exist free of the heterodimer in significant quantities. While anti-heavy subunit antibodies had previously been shown to alter adherence, anti-light subunit antibodies did not, suggesting that the heavy subunit contains the carbohydrate recognition domain. |
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Keywords: | lectin Entamoeba histolytica Entamoeba dispar adherence galactose amebiasis |
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