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Abstract

In nearly all eukaryotic systems, calcium signaling is a crucial component in a number of essential processes. It is accepted that it might likewise be a significant flagging arrangement of the protist parasite Entamoeba histolytica. Ca2+ signaling is thought to be linked to the processes that lead to E. histolytica's invasion and pathogenesis, which include motility, adhesion, cytolysis, phagocytosis, and trogocytosis. There is a huge number of Ca2+ restricting proteins (CaBPs) in E. histolytica, and some of these proteins appear to be related with various strides in pathogenesis. The fact that this parasite's genome contains 27 EF-hand-containing CaBPs in addition to a number of other proteins with Ca2+ binding domains or motif suggests an intricate calcium signaling network. E. histolytica lacks a typical calmodulin like protein, unlike other eukaryotes. None of the CaBPs show grouping closeness with a common calmodulin, broad underlying likeness has been found notwithstanding absence of huge practical crossover with that of average calmodulins. The identification of CaBPs (EhCaBP1, EhCaBP3) that are able to directly bind actin and modulate actin dynamics is one of the distinguishing characteristics of E. histolytica. Direct connection of CaBPs with actin has not been found in some other framework.