EhADH112 Is a Bro1 Domain-Containing Protein Involved in the<i>Entamoeba histolytica</i>Multivesicular Bodies Pathway

Bañuelos, Cecilia; Garcı́a-Rivera, Guillermina; López-Reyes, Israel; Mendoza, Leobardo; González‐Robles, Arturo; Herranz, Silvia; Vincent, Olivier; Orozco, Esther

doi:10.1155/2012/657942

Cited by 29 publications

(59 citation statements)

References 47 publications

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“…The presence of EhADH (one of the two proteins forming the EhCPADH complex) in MVB‐like structures was previously evidenced (Banuelos et al, ; Castellanos‐Castro et al, ). In addition, Castellanos‐Castro et al () showed the co‐localisation of EhADH with lysobisphosphatidic acid, a phospoholipid that in eukaryotes is only detected in late endosomes.…”

Section: Discussionmentioning

confidence: 81%

“…Trophozoites were incubated for 0, 2, 10, 15, 20, 30, and 60 min with RBCs (1:25) at t 37°C for phagocytosis experiments (Banuelos et al, ; Garcia‐Rivera, Sanchez, Orozco, & Guarneros, ) at 37°C for phagocytosis assays or 4°C for adhesion assays for 0, 2, 10, 15, 20, 30, and 60 min. Preparations were quickly washed three times with PBS 1X or TYI‐water (1:1) and prepared for immunofluorescence (Banuelos et al, ; Bolanos et al, ), immunoelectron microscopy, western blot assays, and immunoprecipitation.…”

Section: Methodsmentioning

confidence: 99%

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EhRabB mobilises the EhCPADH complex through the actin cytoskeleton during phagocytosis of Entamoeba histolytica

Javier-Reyna

Montaño

Garcı́a-Rivera

et al. 2019

Cellular Microbiology

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Movement and phagocytosis are clue events in colonisation and invasion of tissues by Entamoeba histolytica, the protozoan causative of human amoebiasis. During phagocytosis, EhRab proteins interact with other functional molecules, conducting them to the precise cellular site. The gene encoding EhrabB is located in the complementary chain of the DNA fragment containing Ehcp112 and Ehadh genes, which encode for the proteins of the EhCPADH complex, involved in phagocytosis. This particular genetic organisation suggests that the three corresponding proteins may be functionally related. Here, we studied the relationship of EhRabB with EhCPADH and actin during phagocytosis. First, we obtained the EhRabB 3D structure to carry out docking analysis to predict the interaction sites involved in the EhRabB protein and the EhCPADH complex contact. By confocal microscopy, transmission electron microscopy, and immunoprecipitation assays, we revealed the interaction among these proteins when they move through different vesicles formed during phagocytosis. The role of the actin cytoskeleton in this event was also confirmed using Latrunculin A to interfere with actin polymerisation. This affected the movement of EhRabB and EhCPADH, as well as the rate of phagocytosis. Mutant trophozoites, silenced in EhrabB gene, evidenced the interaction of this molecule with EhCPADH and strengthened the role of actin during erythrophagocytosis.

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Section: Discussionmentioning

confidence: 81%

Section: Methodsmentioning

confidence: 99%

EhRabB mobilises the EhCPADH complex through the actin cytoskeleton during phagocytosis of Entamoeba histolytica

Javier-Reyna

Montaño

Garcı́a-Rivera

et al. 2019

Cellular Microbiology

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“…histolytica trophozoites lack typical cellular structures present in higher eukaryotes, such as mitochondria, Golgi apparatus and a well-differentiated endoplasmic reticulum (Ghosh et al, 1999). The parasite uses primitive organelles that through a dynamic and complex vesicle trafficking perform their corresponding functions (Bañuelos et al, 2012), which remarks the importance of lipids in virulence. In addition, lipids also work as signaling molecules, energy stores, post-translational modifiers and inclusive, as virulence factors (Shrimal et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

Lipids in Entamoeba histolytica: Host-Dependence and Virulence Factors

Castellanos-Castro

Bolaños

Orozco

2020

Front. Cell. Infect. Microbiol.

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Lipids are essential players in parasites pathogenesis. In particular, the highly phagocytic trophozoites of Entamoeba histolytica, the causative agent of amoebiasis, exhibit a dynamic membrane fusion and fission, in which lipids strongly participate; particularly during the overstated motility of the parasite to reach and attack the epithelia and ingest target cells. Synthesis and metabolism of lipids in this protozoan present remarkable difference with those performed by other eukaryotes. Here, we reviewed the current knowledge on lipids in E. histolytica. Trophozoites synthesize phosphatidylcholine and phosphatidylethanolamine by the Kennedy pathway; and sphingolipids, phosphatidylserine, and phosphatidylinositol, by processes similar to those used by other eukaryotes. However, trophozoites lack enzymes for cholesterol and fatty acids synthesis, which are scavenged from the host or culture medium by specific mechanisms. Cholesterol, a fundamental molecule for the expression of virulence, is transported from the medium into the trophozoites by EhNPC1 and EhNPC2 proteins. Inside cells, lipids are distributed by different pathways, including by the participation of the endosomal sorting complex required for transport (ESCRT), involved in vesicle fusion and fission. Cholesterol interacts with the phospholipid lysobisphosphatidic acid (LBPA) and EhADH, an ALIX family protein, also involved in phagocytosis. In this review, we summarize the known information on phospholipids synthesis and cholesterol transport as well as their metabolic pathways in E. histolytica; highlighting the mechanisms used by trophozoites to dispose lipids involved in the virulence processes.

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“…Overexpressed ADH112 localizes to the plasma membrane and cytoplasmic vesicles and accumulates on MVBs, and can interact with the ESCRT subunit Vps32. Expression of exogenous Bro1 has a dominant negative effect on red blood cell phagocytosis [101], suggesting a possible role for ESCRT machinery in this process.…”

Section: Functional Homology In Trafficking Machinery Between Divermentioning

confidence: 99%

Resolving the homology—function relationship through comparative genomics of membrane-trafficking machinery and parasite cell biology

Klinger

Ramírez-Macías

Herman

et al. 2016

Molecular and Biochemical Parasitology

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With advances in DNA sequencing technology, it is increasingly common and tractable to informatically look for genes of interest in the genomic databases of parasitic organisms and infer cellular states. Assignment of a putative gene function based on homology to functionally characterized genes in other organisms, though powerful, relies on the implicit assumption of functional homology, i.e. that orthology indicates conserved function. Eukaryotes reveal a dazzling array of cellular features and structural organization, suggesting a concomitant diversity in their underlying molecular machinery. Significantly, examples of novel functions for pre-existing or new paralogues are not uncommon. Do these examples undermine the basic assumption of functional homology, especially in parasitic protists, which are often highly derived? Here we examine the extent to which functional homology exists between organisms spanning the eukaryotic lineage. By comparing membrane trafficking proteins between parasitic protists and traditional model organisms, where direct functional evidence is available, we find that function is indeed largely conserved between orthologues, albeit with significant adaptation arising from the unique biological features within each lineage.

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EhADH112 Is a Bro1 Domain-Containing Protein Involved in theEntamoeba histolyticaMultivesicular Bodies Pathway

Cited by 29 publications

References 47 publications

EhRabB mobilises the EhCPADH complex through the actin cytoskeleton during phagocytosis of Entamoeba histolytica

EhRabB mobilises the EhCPADH complex through the actin cytoskeleton during phagocytosis of Entamoeba histolytica

Lipids in Entamoeba histolytica: Host-Dependence and Virulence Factors

Resolving the homology—function relationship through comparative genomics of membrane-trafficking machinery and parasite cell biology

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