Autophosphorylation of Ser428 of EhC2PK Plays a Critical Role in Regulating Erythrophagocytosis in the Parasite Entamoeba histolytica

Somlata,; Kamanna, Sathisha; Agrahari, Mridula; Babuta, Mrigya; Bhattacharya, Sudha; Bhattacharya, Alok

doi:10.1074/jbc.m111.308874

Cited by 16 publications

(18 citation statements)

References 28 publications

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“…6, compare D with A). To validate these observations the levels of fluorescence in cytosol, membrane, and phagocytic cups were quantitated as described (11,48) and the results clearly showed that (Y81F)-EhCaBP1 is significantly more in the membrane region compared with the cytosol (Fig. 6E).…”

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confidence: 99%

Functional Manipulation of a Calcium-binding Protein from Entamoeba histolytica Guided by Paramagnetic NMR

Rout

Patel

Somlata

et al. 2013

Journal of Biological Chemistry

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Background: EhCaBP1 is one of the EF-hand calcium-binding proteins (CaBP) involved in various Ca 2ϩ signaling pathways. Results: Hydrophobic residues at the Ϫ4 position of the Ca 2ϩ -binding loop affects structure, Ca 2ϩ -binding properties, and cellular localization of EhCaBP1. Conclusion: The Y81F mutation in EhCaBP1 makes it more structured like CaM and TnC. Significance: Observed variations in the structures and cellular localization of the wt and mutant could have influence on their biological behavior.

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confidence: 99%

Functional Manipulation of a Calcium-binding Protein from Entamoeba histolytica Guided by Paramagnetic NMR

Rout

Patel

Somlata

et al. 2013

Journal of Biological Chemistry

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“…It has been recently demonstrated that EhCaBP1, a calcium binding protein (Jain et al ., ), the C2 domain‐containing protein kinase, EhC2PK (Somlata et al ., ) and the hypothetical protein (EHI_160980) (King et al ., ) are important regulators of erythrophagocytosis. In addition, the major haemolytic activity of E. histolytica has been associated with an alkaline phospholipase A activity (Vargas‐Villarreal et al ., ).…”

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confidence: 99%

Identification of dihydropyrimidine dehydrogenase as a virulence factor essential for the survival ofEntamoeba histolyticain glucose-poor environments

et al. 2012

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SummaryAdaptation to nutritional changes is a key feature for successful survival of a pathogen within its host. The protozoan parasite Entamoeba histolytica normally colonizes the human colon and in rare occasions, this parasite spread to distant organs, such as the liver. E. histolytica obtains most of its energy from the fermentation of glucose into ethanol. In this study, we were intrigued to know how this parasite reacts to changes in glucose availability and we addressed this issue by performing a DNA microarray analysis of gene expression. Results show that parasites that were adapted to growth in absence of glucose increased their virulence and altered the transcription of several genes. One of these genes is the dihydropyrimidine dehydrogenase (DPD), which is involved in degradation of pyrimidines. We showed that this gene is crucial for the parasite's growth when the availability of glucose is limited. These data contribute to our understanding of the parasite's ability to survive in glucosepoor environments and reveal a new role for the DPD enzyme.

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“…It appears that Ca 2+ plays a critical role as EhC2PK binds the PS-containing inner leafl et of the plasma membrane in the presence of Ca 2+ (for details about Ca 2+ signaling, see chapter on kinases and signaling). The kinase activity of EhC2PK is shown to be essential for the progression of phagocytic cups to the phagosome as overexpression of a kinasedead mutant resulted in a reduction of erythrophagocytosis [ 54 ]. Because the substrate for EhC2PK has not been identifi ed, the nature of the downstream signaling pathway propagated through EhC2PK is not clear.…”

Section: Role Of Ca 2+ In Phagocytosismentioning

confidence: 99%

Phagocytosis in Entamoeba histolytica

Somlata¹,

Bhattacharya²

2014

Amebiasis

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Phagocytosis is one of the essential processes that is necessary for the survival and pathogenicity of Entamoeba histolytica. E. histolytica is known to phagocytose red blood cells (RBC), bacteria and other unicellular organisms, immune cells, and apoptotic cells during either proliferation in the gut or invasion in intestinal and extraintestinal tissues. Molecular pathways are not clear about molecular details in E. histolytica and are thought to be different from those known in other systems. In this chapter we describe our current understanding of molecular mechanisms of phagocytosis in E. histolytica and highlight new avenues for research for future drug development.

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Autophosphorylation of Ser428 of EhC2PK Plays a Critical Role in Regulating Erythrophagocytosis in the Parasite Entamoeba histolytica

Cited by 16 publications

References 28 publications

Functional Manipulation of a Calcium-binding Protein from Entamoeba histolytica Guided by Paramagnetic NMR

Functional Manipulation of a Calcium-binding Protein from Entamoeba histolytica Guided by Paramagnetic NMR

Identification of dihydropyrimidine dehydrogenase as a virulence factor essential for the survival ofEntamoeba histolyticain glucose-poor environments

Phagocytosis in Entamoeba histolytica

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