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A subunit vaccine candidate region of the Entamoeba histolytica galactose‐adherence lectin promotes interleukin‐12 gene transcription and protein production in human macrophages

The cysteine‐rich region of the 170‐kDa subunit galactose‐adherence lectin (Gal‐lectin) of Entamoeba histolytica is a subunit vaccine candidate and a protective antigen in the gerbil model of amebiasis. Macrophage‐mediated immunity is important for protection against E. histolytica and is activated by Th1 cytokines. As Th1 differentiation is promoted by IL‐12, we investigated what portion of the Gal‐lectin could stimulate IL‐12 in human THP‐1 macrophages. Native Gal‐lactin stimulated IL‐12 p40 / p35 mRNA expression in a dose‐ and time‐dependent manner as measured by reverse transcriptase‐PCR. Human immune serum and Gal‐lectin mAb inhibition studies identified amino acids (aa) 596 – 998 as immunogenic and containing the IL‐12 inducing domain. IFN‐γ priming augmented Gal‐lectin‐induced IL‐12 mRNA expression independent of TNF‐α and IL‐1β, and was required for IL‐12 p70 protein production from macrophages and human peripheral blood mononuclear cells. Gal‐lectin plus IFN‐γ stimulated IL‐12 p40 and p35 gene transcription with stable mRNA transcripts and a differential requirement for protein synthesis. These results suggest that aa 596 – 998 of the Gal‐lectin can confer Th1‐mediated protection against amebiasis through IL‐12 induction.