ArticlePLoS pathogens2015
EhVps32 Is a Vacuole-Associated Protein Involved in Pinocytosis and Phagocytosis of Entamoeaba histolytica.
Article in PLoS pathogens, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- EhVps29 Has a Role in the Location of the Retromer Complex and the Function of Key Virulence Factors inMicroorganisms · 2026Article
- EhVps35, a retromer component, is involved in the recycling of the EhADH and Gal/GalNac virulent proteins ofFrontiers in parasitology · 2024Article
- EhVps35, a retromer component, is a key factor in secretion, motility, and tissue invasion byFrontiers in cellular and infection microbiology · 2024Article
- The Entamoeba histolytica Vps26 (EhVps26) retromeric protein is involved in phagocytosis: Bioinformatic and experimental approaches.PloS one · 2024Article
- Dynamic Association of ESCRT-II Proteins with ESCRT-I and ESCRT-III Complexes during Phagocytosis ofInternational journal of molecular sciences · 2023Article
- Stepwise remodeling and subcompartment formation in individual vesicles by three ESCRT-III proteins.iScience · 2023Article
- Molecular interplays of theFrontiers in cellular and infection microbiology · 2022Review
- EhVps23, an ESCRT-I Member, Is a Key Factor in Secretion, Motility, Phagocytosis and Tissue Invasion byFrontiers in cellular and infection microbiology · 2022Article
- Protein Sumoylation Is Crucial for Phagocytosis inInternational journal of molecular sciences · 2021Article
- Two StAR-related lipid transfer proteins play specific roles in endocytosis, exocytosis, and motility in the parasitic protist Entamoeba histolytica.PLoS pathogens · 2021Article
- EhVps23: A Component of ESCRT-I That Participates in Vesicular Trafficking and Phagocytosis ofFrontiers in cellular and infection microbiology · 2021Article
- Review
- The Entamoeba histolytica TBP and TRF1 transcription factors are GAAC-box binding proteins, which display differential gene expression under different stress stimuli and during the interaction with mammalian cells.Parasites & vectors · 2018Article
- Epithelial Cells Expressing EhADH, AnFrontiers in cellular and infection microbiology · 2018Article
- Non-vesicular Lipid Transport Machinery inFrontiers in cellular and infection microbiology · 2018Review
- The Conserved ESCRT-III Machinery Participates in the Phagocytosis ofFrontiers in cellular and infection microbiology · 2018Article
- Article
- EhNPC1 and EhNPC2 Proteins Participate in Trafficking of Exogenous Cholesterol in Entamoeba histolytica Trophozoites: Relevance for Phagocytosis.PLoS pathogens · 2016Article
- Identification of the phospholipid lysobisphosphatidic acid in the protozoanBiochemistry and biophysics reports · 2016Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Here, we investigated the role of EhVps32 protein (a member of the endosomal-sorting complex required for transport) in endocytosis of Entamoeba histolytica, a professional phagocyte. Confocal microscopy, TEM and cell fractionation revealed EhVps32 in cytoplasmic vesicles and also located adjacent to the plasma membrane. Between 5 to 30 min of phagocytosis, EhVps32 was detected on some erythrocytes-containing phagosomes of acidic nature, and at 60 min it returned to cytoplasmic vesicles and also appeared adjacent to the plasma membrane. TEM images revealed it in membranous structures in the vicinity of ingested erythrocytes. EhVps32, EhADH (an ALIX family member), Gal/GalNac lectin and actin co-localized in the phagocytic cup and in some erythrocytes-containing phagosomes, but EhVps32 was scarcely detected in late phagosomes. During dextran uptake, EhVps32, EhADH and Gal/GalNac lectin, but not actin, co-localized in pinosomes. EhVps32 recombinant protein formed oligomers composed by rings and filaments. Antibodies against EhVps32 monomers stained cytoplasmic vesicles but not erythrocytes-containing phagosomes, suggesting that in vivo oligomers are formed on phagosome membranes. The involvement of EhVps32 in phagocytosis was further study in pNeoEhvps32-HA-transfected trophozoites, which augmented almost twice their rate of erythrophagocytosis as well as the membranous concentric arrays built by filaments, spirals and tunnel-like structures. Some of these structures apparently connected phagosomes with the phagocytic cup. In concordance, the EhVps32-silenced G3 trophozoites ingested 80% less erythrocytes than the G3 strain. Our results suggest that EhVps32 participates in E. histolytica phagocytosis and pinocytosis. It forms oligomers on erythrocytes-containing phagosomes, probably as a part of the scission machinery involved in membrane invagination and intraluminal vesicles formation.
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