Glycoconjugate Journal

, Volume 11, Issue 5, pp 432–436 | Cite as

Use of monoclonal anti-light subunit antibodies to study the structure and function of theEntamoeba histolytica Gal/GalNAc adherence lectin

  • James J. McCoy
  • Alissa M. Weaver
  • William A. PetriJr
Lectin Papers


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.


lectin Entamoeba histolytica Entamoeba dispar adherence galactose amebiasis 


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Copyright information

© Chapman & Hall 1994

Authors and Affiliations

  • James J. McCoy
    • 1
  • Alissa M. Weaver
    • 1
  • William A. PetriJr
    • 1
  1. 1.From the Departments of Medicine, Microbiology and PathologyUniversity of Virginia School of MedicineCharlottesvilleUSA

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