Open AccessEntamoeba histolytica and pathogenesis: A calcium connection
Author(s) -
Mrigya Babuta,
Sudha Bhattacharya,
Alok Bhattacharya
Publication year - 2020
Publication title -
plos pathogens
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.719
H-Index - 206
eISSN - 1553-7374
pISSN - 1553-7366
DOI - 10.1371/journal.ppat.1008214
Subject(s) - entamoeba histolytica , biology , microbiology and biotechnology , actin , motility , calcium binding protein , calcium signaling , calmodulin , signal transduction , calcium , biochemistry , chemistry , enzyme , organic chemistry
Calcium signaling plays a key role in many essential processes in almost all eukaryotic systems. It is believed that it may also be an important signaling system of the protist parasite Entamoeba histolytica . Motility, adhesion, cytolysis, and phagocytosis/trogocytosis are important steps in invasion and pathogenesis of E . histolytica , and Ca 2+ signaling is thought to be associated with these processes leading to tissue invasion. There are a large number of Ca 2+ -binding proteins (CaBPs) in E . histolytica , and a number of these proteins appear to be associated with different steps in pathogenesis. The genome encodes 27 EF-hand–containing CaBPs in addition to a number of other Ca 2+ -binding domain/motif-containing proteins, which suggest intricate calcium signaling network in this parasite. Unlike other eukaryotes, a typical calmodulin-like protein has not been seen in E . histolytica . Though none of the CaBPs display sequence similarity with a typical calmodulin, extensive structural similarity has been seen in spite of lack of significant functional overlap with that of typical calmodulins. One of the unique features observed in E . histolytica is the identification of CaBPs (EhCaBP1, EhCaBP3) that have the ability to directly bind actin and modulate actin dynamics. Direct interaction of CaBPs with actin has not been seen in any other system. Pseudopod formation and phagocytosis are some of the processes that require actin dynamics, and some of the amoebic CaBPs (EhC2Pk, EhCaBP1, EhCaBP3, EhCaBP5) participate in this process. None of these E . histolytica CaBPs have any homolog in organisms other than different species of Entamoeba, suggesting a novel Ca 2+ signaling pathway that has evolved in this genus.