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Review
. 2014;10(6):1514-21.
doi: 10.4161/hv.27796. Epub 2014 Feb 6.

The future for vaccine development against Entamoeba histolytica

Jeanie Quach  1 , Joëlle St-Pierre  1 , Kris Chadee  1
Affiliations
Review

The future for vaccine development against Entamoeba histolytica

Jeanie Quach et al. Hum Vaccin Immunother. 2014.

Abstract

Entamoeba histolytica is the causative agent of amebiasis, one of the top three parasitic causes of mortality worldwide. In the majority of infected individuals, E. histolytica asymptomatically colonizes the large intestine, while in others, the parasite breaches the mucosal epithelial barrier to cause amebic colitis and can disseminate to soft organs to cause abscesses. Vaccinations using native and recombinant forms of the parasite Gal-lectin have been successful in protecting animals against intestinal amebiasis and amebic liver abscess. Protection against amebic liver abscesses has also been reported by targeting other E. histolytica components including the serine-rich protein and the 29-kDa-reductase antigen. To date, vaccines against the Gal-lectin hold the most promise but clinical trials will be required to validate its efficacy in humans. Here, we review the current strategies and future perspectives involved in the development of a vaccine against E. histolytica.

Keywords: DNA vaccine; Entamoeba histolytica; amebiasis; amebic colitis; amebic liver abscess; cell-mediated immunity; dysentery; immune response; immunopathogenesis; mucosal immune response.

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Figures

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Figure 1. A schematic structure of the E. histolytica Gal-lectin. The Gal-lectin adhesin is composed of 3 subunits: the heavy subunit (Hgl) is linked by disulfide bonds to the light subunit (Lgl) and is non-covalently associated with the intermediate subunit (Igl). The heavy subunit has a short cytoplasmic tail and both the light and intermediate subunits are GPI anchored. TM, transmembrane; CD, cytoplasmic domain; CRD, carbohydrate rich domain; GPI, glycosylphosphatidylinisotol.
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