Molecular Basis of Pathogenesis in Amoebiasis

Abstract

Amoebiasis is one of the major public health problems in developing countries. In spite of the availability of an effective drug and absence of overt drug resistance, the disease is still prevalent among large population and spread over a number of countries. It is caused by the protist parasite Entamoeba histolytica that essentially infects humans, though other species that infect a few animals have been reported. A number of molecular techniques have recently been developed. These have helped in understanding biological processes in E. histolytica and in the identification of key molecules that are involved in amoebic virulence and invasion. Moreover, developments in the area of disease and invasion models have allowed understanding of these processes at molecular level and circumvented lack of a good animal model of amoebiasis. All these knowledge will help us to design better therapeutics and allow us to control this important disease.

Review Article: Amebiasis Molecular Pathogenesis Development

“…HgI and LgI are connected via disulfide bonds and live on the parasite cell membrane as a 260kDa heterodimer. HgI contains carbohydrate recognition domain (CRD) which recognizes d-galactose and N-acetyl-dgalactosamine and host cell glycoconjugate proteins (3,12) .…”

“…Cell contact is the beginning of invasion of E. histolytica. Amoeba also attacks by reducing or damaging tissue by secreting several enzymes capable of digesting tissues or even extracellular matrices (12) .…”

“…EhCP5 is also associated with colon epithelial cell integrins and activates the NFkappaβ-mediated inflammatory response in host cells. Research in 2014 showed that EhCPA5 activates matrix metalloproteinase (MMP) by splitting (12,13) .…”

“…Amoebapores is a group of pore-forming peptides that mediate the killing of cells by acting as secreted toxins. Amoebapores has 3 different types (a, b, and c) which structurally and functionally similar to NK-lysin membrane and granulysin permeabilization proteins produced by mammalian T cells (11,12) . All amoebapores induce pore formation in synthetic liposomes.…”

“…Other calcium binding proteins such as EhCaBP3 interact directly with lipids and function in the initiation of independent phagocytosis from the EhCaBP1/EhC2PK pathway. Whereas EhCaBP5, has recently been shown to interact with myosin 1B in an independent manner of calcium (11,12) .…”