Abstract
The parasite Entamoeba histolytica is the etiological agent of amoebiasis and phagocytosis plays a key role in virulence of this organism. Signaling pathways involved in activation of cytoskeletal dynamics required for phagocytosis remain to be elucidated. Phagocytosis is initiated with sequential recruitment of EhC2PK, EhCaBP1, EhCaBP3 and an atypical kinase EhAK1 after particle attachment. Here we show that EhARPC1, an essential subunit of the actin branching complex Arp 2/3 is recruited to the phagocytic initiation sites by EhAK1. Imaging, expression knockdown of different molecules and pull down experiments suggest that EhARPC1 interacts with EhAK1 and that it is required during initiation of phagocytosis and phagosome formation. Moreover, recruitment of EhARPC2 at the phagocytosis initiation by EhAK1 is also observed, indicating that the Arp 2/3 complex is recruited. In conclusion, these results suggests a novel mechanism of recruitment of Arp 2/3 complex during phagocytosis in E. histolytica.
Highlights
Phagocytosis plays a critical role in invasion and pathogenesis of the parasite Entamoeba histolytica, the causative agent of amoebiasis, and a major cause of morbidity and mortality in developing countries
E. histolytica is the causative agent of amoebiasis and leads to morbidity and mortality in developing countries
We have been investigating this pathway by using red blood cells as a particle and have identified different molecules required during the initial stages of phagocytosis
Summary
Phagocytosis plays a critical role in invasion and pathogenesis of the parasite Entamoeba histolytica, the causative agent of amoebiasis, and a major cause of morbidity and mortality in developing countries. Arp2/3 complex is one of the main group of molecules required for actin dynamics. It comprises of seven subunits, Actin related protein 2 (Arp2, 44KDa), Actin related protein 3 (Arp3, 47KDa), ARPC1 (40KDa), ARPC2 (35KDa), ARPC3 (21KDa), ARPC4 (20KDa) and ARPC5 (16KDa). There are multiple ways by which Arp 2/3 complex is recruited at the site of actin dynamics. Some of the examples are, interaction with VCA domain of activated NPFs (nucleation protein factors) [6], direct binding of Arp2/3 complex to vinculin (an integrin associated protein) during cell migration at the sites of integrinmediated adhesions and membrane protrusions and binding of F-actin [7], direct binding to cortical actin associated protein (cortactin) [8] and recruitment through WAVE2 complex during T-cell activation [9]. We can conclude from this discussion that there are multiple ways by which Arp 2/3 complex gets activated in different systems
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