A Recombinant Cysteine-Rich Section Of The Entamoeba Histolytica Galactoseinhibitable Lectin Is Efficacious As A Subunit Vaccine In The Gerbil Model Of Amebic Liver Abscess

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Abstract
The 170-kDa subunit of the galactose-inhibitable adherence lectin of Entamoeba histolytica mediates attachment to colonic mucins and host cells. The DNA fragment encoding the 170-kDa subunit was produced by polymerase chain reaction (PCR) and divided into four sections by restriction endonucleases. The third section (designated LC3, base pairs 2273–3397) encodes a cysteine-rich fusion protein that was recognized by adherence-inhibitory anti-lectin monoclonal antibodies and serum antibodies from 95% of subjects with amebic liver abscess. Immunization of gerbils with purified recombinant LC3-encoded protein (10 µg) with Titermax adjuvant elicited a high-titer serum anti-LC3 IgG antibody response and protective immunity against intrahepatic challenge with 0.5 'd7 106 virulent axenic trophozoites (strain HM1:IMSS; 71% vaccine efficacy, P < .01). In summary, a recombinant cysteine-rich portion of the 170-kDa lectin subunit was highly antigenic, immunogenic, and effectiveas a subunit vaccine in an experimental animal model of amebic liver abscess.

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