{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T19:44:43Z","timestamp":1777578283436,"version":"3.51.4"},"reference-count":79,"publisher":"MDPI AG","issue":"14","license":[{"start":{"date-parts":[[2024,7,11]],"date-time":"2024-07-11T00:00:00Z","timestamp":1720656000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003141","name":"National Council for Science and Technology (Conacyt)","doi-asserted-by":"publisher","award":["A1-S8380"],"award-info":[{"award-number":["A1-S8380"]}],"id":[{"id":"10.13039\/501100003141","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Entamoeba histolytica is the protozoan causative of human amoebiasis. The EhADH adhesin (687 aa) is a protein involved in tissue invasion, phagocytosis and host-cell lysis. EhADH adheres to the prey and follows its arrival to the multivesicular bodies. It is an accessory protein of the endosomal sorting complexes required for transport (ESCRT) machinery. Here, to study the role of different parts of EhADH during virulence events, we produced trophozoites overexpressing the three domains of EhADH, Bro1 (1\u2013400 aa), Linker (246\u2013446 aa) and Adh (444\u2013687 aa) to evaluate their role in virulence. The TrophozBro11\u2013400 slightly increased adherence and phagocytosis, but these trophozoites showed a higher ability to destroy cell monolayers, augment the permeability of cultured epithelial cells and mouse colon, and produce more damage to hamster livers. The TrophozLinker226\u2013446 also increased the virulence properties, but with lower effect than the TrophozBro11\u2013400. In addition, this fragment participates in cholesterol transport and GTPase binding. Interestingly, the TrophozAdh444\u2013687 produced the highest effect on adherence and phagocytosis, but it poorly influenced the monolayers destruction; nevertheless, they augmented the colon and liver damage. To identify the protein partners of each domain, we used recombinant peptides. Pull-down assays and mass spectrometry showed that Bro1 domain interplays with EhADH, Gal\/GalNAc lectin, EhCPs, ESCRT machinery components and cytoskeleton proteins. While EhADH, ubiquitin, EhRabB, EhNPC1 and EhHSP70 were associated to the Linker domain, and EhADH, EhHSP70, EhPrx and metabolic enzymes interacted to the Adh domain. The diverse protein association confirms that EhADH is a versatile molecule with multiple functions probably given by its capacity to form distinct molecular complexes.<\/jats:p>","DOI":"10.3390\/ijms25147609","type":"journal-article","created":{"date-parts":[[2024,7,12]],"date-time":"2024-07-12T08:47:41Z","timestamp":1720774061000},"page":"7609","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Entamoeba histolytica: EhADH, an Alix Protein, Participates in Several Virulence Events through Its Different Domains"],"prefix":"10.3390","volume":"25","author":[{"given":"Dxinegueela","family":"Zanatta","sequence":"first","affiliation":[{"name":"Department of Infectomics and Molecular Pathogenesis, Center for Research and Advanced Studies of National Polytechnic Institute, Mexico City 07360, Mexico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1761-0481","authenticated-orcid":false,"given":"Abigail","family":"Betanzos","sequence":"additional","affiliation":[{"name":"Department of Infectomics and Molecular Pathogenesis, Center for Research and Advanced Studies of National Polytechnic Institute, Mexico City 07360, Mexico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6392-170X","authenticated-orcid":false,"given":"Elisa","family":"Azuara-Liceaga","sequence":"additional","affiliation":[{"name":"Postgraduate in Genomic Sciences, Autonomous University of Mexico City, Mexico City 03100, Mexico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0420-4268","authenticated-orcid":false,"given":"Sarita","family":"Monta\u00f1o","sequence":"additional","affiliation":[{"name":"Laboratory of Bioinformatics and Molecular Simulation, Faculty of Biological Chemistry Sciences, Autonomous University of Sinaloa, Sinaloa 80030, Mexico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8360-2968","authenticated-orcid":false,"given":"Esther","family":"Orozco","sequence":"additional","affiliation":[{"name":"Department of Infectomics and Molecular Pathogenesis, Center for Research and Advanced Studies of National Polytechnic Institute, Mexico City 07360, Mexico"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2024,7,11]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Mor\u00e1n, P., Serrano-V\u00e1zquez, A., Rojas-Vel\u00e1zquez, L., Gonz\u00e1lez, E., P\u00e9rez-Ju\u00e1rez, H., Hern\u00e1ndez, E.G., Padilla, M.d.L.A., Zaragoza, M.E., Portillo-Bobadilla, T., and Ramiro, M. (2023). Amoebiasis: Advances in Diagnosis, Treatment, Immunology Features and the Interaction with the Intestinal Ecosystem. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms241411755"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"ofy161","DOI":"10.1093\/ofid\/ofy161","article-title":"A review of the global burden, new diagnostics, and current therapeutics for amebiasis","volume":"5","author":"Shirley","year":"2018","journal-title":"Open Forum Infect. Dis."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"4601420","DOI":"10.1155\/2018\/4601420","article-title":"Entamoeba Histolytica: Updates in Clinical Manifestation, Pathogenesis, and Vaccine Development","volume":"2018","author":"Kantor","year":"2018","journal-title":"Can. J. Gastroenterol. Hepatol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"272","DOI":"10.4329\/wjr.v14.i8.272","article-title":"Amebic liver abscess: Clinico-radiological findings and interventional management","volume":"14","author":"Priyadarshi","year":"2022","journal-title":"World J. Radiol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1016\/j.pt.2011.02.006","article-title":"Tissue destruction and invasion by Entamoeba histolytica","volume":"27","author":"Ralston","year":"2011","journal-title":"Trends Parasitol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1152\/physiol.00038.2019","article-title":"Immune response to the enteric parasite Entamoeba histolytica","volume":"35","author":"Rosales","year":"2020","journal-title":"Physiology"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"556","DOI":"10.1046\/j.1365-2958.1999.01500.x","article-title":"Entamoeba histolytica: A novel cysteine protease and an adhesin form the 112 kDa surface protein","volume":"33","author":"Arroyo","year":"1999","journal-title":"Mol. Microbiol."},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Betanzos, A., Javier-Reyna, R., Garc\u00eda-Rivera, G., Ba\u00f1uelos, C., Gonz\u00e1lez-Mariscal, L., Schnoor, M., and Orozco, E. (2013). The EhCPADH112 Complex of Entamoeba histolytica Interacts with Tight Junction Proteins Occludin and Claudin-1 to Produce Epithelial Damage. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0065100"},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Cuellar, P., Hern\u00e1ndez-Nava, E., Garc\u00eda-Rivera, G., Ch\u00e1vez-Mungu\u00eda, B., Schnoor, M., Betanzos, A., and Orozco, E. (2017). Entamoeba histolytica EhCP112 dislocates and degrades claudin-1 and claudin-2 at tight junctions of the intestinal epithelium. Front. Cell. Infect. Microbiol., 7.","DOI":"10.3389\/fcimb.2017.00372"},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Cornick, S., Moreau, F., and Chadee, K. (2016). Entamoeba histolytica Cysteine Proteinase 5 Evokes Mucin Exocytosis from Colonic Goblet Cells via \u03b1v\u03b23 Integrin. PLOS Pathog., 12.","DOI":"10.1371\/journal.ppat.1005579"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1016\/j.ajpath.2011.05.001","article-title":"Prostaglandin E2 produced by Entamoeba histolytica signals via Ep4 receptor and alters claudin-4 to increase ion permeability of tight junctions","volume":"179","author":"Lejeune","year":"2011","journal-title":"Am. J. Pathol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"4176","DOI":"10.1016\/j.vaccine.2009.04.051","article-title":"A pcDNA-Ehcpadh vaccine against Entamoeba histolytica elicits a protective Th1-like response in hamster liver","volume":"27","author":"Aguilar","year":"2009","journal-title":"Vaccine"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1080\/07391102.2016.1151831","article-title":"Heterodimerization of the Entamoeba histolytica EhCPADH virulence complex through molecular dynamics and protein\u2013protein docking","volume":"35","author":"Orozco","year":"2017","journal-title":"J. Biomol. Struct. Dyn."},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Ba\u00f1uelos, C., Garc\u00eda-Rivera, G., L\u00f3pez-Reyes, I., Mendoza, L., Gonz\u00e1lez-Robles, A., Herranz, S., Vincent, O., and Orozco, E. (2012). EhADH112 is a Bro1 domain-containing protein involved in the Entamoeba histolytica multivesicular bodies pathway. J. Biomed. Biotechnol., 2012.","DOI":"10.1155\/2012\/657942"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.tcb.2013.10.009","article-title":"ALIX and the multivesicular endosome: ALIX in Wonderland","volume":"24","author":"Bissig","year":"2014","journal-title":"Trends Cell Biol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"3025","DOI":"10.1242\/jcs.03072","article-title":"The multiple personalities of Alix","volume":"119","author":"Odorizzi","year":"2006","journal-title":"J. Cell Sci."},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Galindo, A., Javier-Reyna, R., Garc\u00eda-Rivera, G., Ba\u00f1uelos, C., Monta\u00f1o, S., Ortega-Lopez, J., Ch\u00e1vez-Mungu\u00eda, B., Salazar-Villatoro, L., and Orozco, E. (2021). EhVps23: A Component of ESCRT-I That Participates in Vesicular Trafficking and Phagocytosis of Entamoeba histolytica. Front. Cell. Infect. Microbiol., 11.","DOI":"10.3389\/fcimb.2021.770759"},{"key":"ref_18","doi-asserted-by":"crossref","unstructured":"L\u00f3pez-Reyes, I., Garc\u00eda-Rivera, G., Ba\u00f1uelos, C., Herranz, S., Vincent, O., L\u00f3pez-Camarillo, C., Marchat, L.A., and Orozco, E. (2010). Detection of the Endosomal Sorting Complex Required for Transport in Entamoeba histolytica and Characterization of the EhVps4 Protein. J. Biomed. Biotechnol., 2010.","DOI":"10.1155\/2010\/890674"},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Avalos-Padilla, Y., Knorr, R.L., Javier-Reyna, R., Garc\u00eda-Rivera, G., Lipowsky, R., Dimova, R., and Orozco, E. (2018). The conserved ESCRT-III machinery participates in the phagocytosis of Entamoeba histolytica. Front. Cell. Infect. Microbiol., 8.","DOI":"10.3389\/fcimb.2018.00053"},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Bola\u00f1os, J., Betanzos, A., Javier-Reyna, R., Rivera, G.G., Huerta, M., Pais-Morales, J., Gonz\u00e1lez-Robles, A., Rodr\u00edguez, M.A., Schnoor, M., and Orozco, E. (2016). EhNPC1 and EhNPC2 Proteins Participate in Trafficking of Exogenous Cholesterol in Entamoeba histolytica Trophozoites: Relevance for Phagocytosis. PLOS Pathog., 12.","DOI":"10.1371\/journal.ppat.1006089"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"16319","DOI":"10.1096\/fj.202001562R","article-title":"Occludin, caveolin-1, and Alix form a multi-protein complex and regulate HIV-1 infection of brain pericytes","volume":"34","author":"Torices","year":"2020","journal-title":"FASEB J."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1093\/bib\/bbr042","article-title":"Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium","volume":"12","author":"Gaudet","year":"2011","journal-title":"Brief. Bioinform."},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Dom\u00ednguez-Fern\u00e1ndez, T., Rodr\u00edguez, M.A., Monroy, V.S., Garc\u00eda, C.G., Medel, O., and Ishiwara, D.G.P. (2018). A Calpain-Like Protein Is Involved in the Execution Phase of Programmed Cell Death of Entamoeba histolytica. Front. Cell. Infect. Microbiol., 8.","DOI":"10.3389\/fcimb.2018.00339"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/S0014-5793(00)02245-6","article-title":"Two novel calcium-binding proteins from cytoplasmic granules of the protozoan parasite Entamoeba histolytica","volume":"486","author":"Nickel","year":"2000","journal-title":"FEBS Lett."},{"key":"ref_25","first-page":"221","article-title":"EhCP112 is an Entamoeba histolytica secreted cysteine protease that may be involved in the parasite-virulence","volume":"7","author":"Orozco","year":"2005","journal-title":"Cell. Microbiol."},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"D\u00edaz-Hern\u00e1ndez, M., Javier-Reyna, R., Mart\u00ednez-Valencia, D., Monta\u00f1o, S., and Orozco, E. (2023). Dynamic Association of ESCRT-II Proteins with ESCRT-I and ESCRT-III Complexes during Phagocytosis of Entamoeba histolytica. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24065267"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"3936","DOI":"10.1016\/S0021-9258(18)32757-1","article-title":"Isolation and characterization of actin from Entamoeba histolytica","volume":"258","author":"Meza","year":"1983","journal-title":"J. Biol. Chem."},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Manich, M., Hernandez-Cuevas, N., Ospina-Villa, J.D., Syan, S., Marchat, L.A., Olivo-Marin, J.C., and Guill\u00e9n, N. (2018). Morphodynamics of the actin-rich cytoskeleton in Entamoeba histolytica. Front. Cell. Infect. Microbiol., 8.","DOI":"10.3389\/fcimb.2018.00179"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1361","DOI":"10.1002\/prot.25955","article-title":"The actin cytoskeleton orchestra in Entamoeba histolytica","volume":"88","author":"Rath","year":"2020","journal-title":"Proteins Struct. Funct. Bioinform."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"D898","DOI":"10.1093\/nar\/gkab929","article-title":"VEuPathDB: The eukaryotic pathogen, vector and host bioinformatics resource center","volume":"50","author":"Amos","year":"2022","journal-title":"Nucleic Acids Res."},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"The UniProt Consortium (2023). UniProt: The Universal Protein Knowledgebase in 2023. Nucleic Acids Res., 51, D523\u2013D531.","DOI":"10.1093\/nar\/gkac1052"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"e15","DOI":"10.1038\/emm.2013.30","article-title":"G protein signaling in the parasite Entamoeba histolytica","volume":"45","author":"Bosch","year":"2013","journal-title":"Exp. Mol. Med."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1016\/j.exppara.2005.02.021","article-title":"The diversity of Rab GTPases in Entamoeba histolytica","volume":"110","author":"Loftus","year":"2005","journal-title":"Exp. Parasitol."},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Saito-Nakano, Y., Wahyuni, R., Nakada-Tsukui, K., Tomii, K., and Nozaki, T. (2021). Rab7D small GTPase is involved in phago-, trogocytosis and cytoskeletal reorganization in the enteric protozoan Entamoeba histolytica. Cell. Microbiol., 23.","DOI":"10.1111\/cmi.13267"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1016\/S0166-6851(02)00047-6","article-title":"Characterization of a Rab7-like GTPase, EhRab7: A marker for the early stages of endocytosis in Entamoeba histolytica","volume":"121","author":"Welter","year":"2002","journal-title":"Mol. Biochem. Parasitol."},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Babuta, M., Bhattacharya, S., and Bhattacharya, A. (2020). Entamoeba histolytica and pathogenesis: A calcium connection. PLOS Pathog., 16.","DOI":"10.1371\/journal.ppat.1008214"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1146\/annurev.nu.15.070195.000343","article-title":"Regulation of tight-junction permeability during nutrient absorption across the intestinal epithelium","volume":"15","author":"Ballard","year":"1995","journal-title":"Annu. Rev. Nutr."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1152\/physrev.00035.2003","article-title":"Endothelial cell-to-cell junctions: Molecular organization and role in vascular homeostasis","volume":"84","author":"Bazzoni","year":"2004","journal-title":"Physiol. Rev."},{"key":"ref_39","first-page":"G467","article-title":"Tight junctions and the molecular basis for regulation of paracellular permeability","volume":"269","author":"Anderson","year":"1995","journal-title":"Am. J. Physiol. Liver Physiol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1007\/BF01870778","article-title":"Tight junction formation in cultured epithelial cells (MDCK)","volume":"86","author":"Cereijido","year":"1985","journal-title":"J. Membr. Biol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1016\/S1046-2023(03)00029-X","article-title":"Functional analysis of tight junctions","volume":"30","author":"Matter","year":"2003","journal-title":"Methods"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"852","DOI":"10.1016\/j.ajpath.2012.11.035","article-title":"Entamoeba histolytica exacerbates epithelial tight junction permeability and proinflammatory responses in Muc2\u2212\/\u2212 mice","volume":"182","author":"Moreau","year":"2013","journal-title":"Am. J. Pathol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"38","DOI":"10.3109\/00365529409090435","article-title":"Evans blue permeation of intestinal mucosa in the rat","volume":"29","author":"Lange","year":"1994","journal-title":"Scand. J. Gastroenterol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1007\/BF00932422","article-title":"Passive immunization during experimental amebic liver-abscess development","volume":"81","author":"Tsutsumi","year":"1995","journal-title":"Parasitol. Res."},{"key":"ref_45","first-page":"1","article-title":"Amebic liver abscess: A diagnostic challenge","volume":"16","author":"Dasrathy","year":"1995","journal-title":"Trop. Gastroenterol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1016\/S1369-5274(99)80076-9","article-title":"Virulence factors of Entamoeba histolytica","volume":"2","author":"Gilchrist","year":"1999","journal-title":"Curr. Opin. Microbiol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1111\/j.0141-9838.2004.00706.x","article-title":"Entamoeba histolytica cysteine protease 2 (EhCP2) modulates leucocyte migration by proteolytic cleavage of chemokines","volume":"26","author":"Belloso","year":"2004","journal-title":"Parasite Immunol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1111\/j.1365-2958.2009.06672.x","article-title":"Major cysteine peptidases of Entamoeba histolytica are required for aggregation and digestion of erythrocytes but are dispensable for phagocytosis and cytopathogenicity","volume":"72","author":"Irmer","year":"2009","journal-title":"Mol. Microbiol."},{"key":"ref_49","first-page":"890603","article-title":"Proteases from Entamoeba spp. and Pathogenic Free-Living Amoebae as Virulence Factors","volume":"2013","year":"2013","journal-title":"J. Trop. Med."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"5294","DOI":"10.1091\/mbc.e05-04-0283","article-title":"A retromerlike complex is a novel Rab7 effector that is involved in the transport of the virulence factor cysteine protease in the enteric protozoan parasite Entamoeba histolytica","volume":"16","author":"Ali","year":"2005","journal-title":"Mol. Biol. Cell"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1016\/0378-1119(94)90299-2","article-title":"Cloning, genomic organization and transcription of the Entamoeba histolytica \u03b1-tubulin-encodmg gene","volume":"146","author":"Peattie","year":"1994","journal-title":"Gene"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1080\/21541248.2018.1528840","article-title":"Rab GTPases take centre stage in understanding Entamoeba histolytica biology","volume":"11","author":"Verma","year":"2020","journal-title":"Small GTPases"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/j.molbiopara.2004.09.002","article-title":"Histone acetyltransferases and deacetylase in Entamoeba histolytica","volume":"138","author":"Ramakrishnan","year":"2004","journal-title":"Mol. Biochem. Parasitol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.actatropica.2011.12.007","article-title":"Obtaining of three recombinant antigens of Entamoeba histolytica and evaluation of their immunogenic ability without adjuvant in a hamster model of immunoprotection","volume":"122","year":"2012","journal-title":"Acta Trop."},{"key":"ref_55","first-page":"7","article-title":"Entamoeba histolytica: cDNAs cloned as 30kDa collagen-binding proteins (CBP) belong to an antioxidant molecule family: Protection of hamsters from amoebic liver abscess by immunization with recombinant CBP","volume":"108","author":"Chaudhuri","year":"2004","journal-title":"Exp. Parasitol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1006\/mpat.1998.0202","article-title":"The pyruvate:ferredoxin oxidoreductase enzyme is located in the plasma membrane and in a cytoplasmic structure in Entamoeba","volume":"25","author":"Mendoza","year":"1998","journal-title":"Microb. Pathog."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1016\/j.febslet.2012.11.020","article-title":"The bifunctional aldehyde-alcohol dehydrogenase controls ethanol and acetate production in Entamoeba histolytica under aerobic conditions","volume":"587","author":"Pineda","year":"2013","journal-title":"FEBS Lett."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"925","DOI":"10.1016\/j.ejcb.2006.04.002","article-title":"Trafficking and developmental signaling: Alix at the crossroads","volume":"85","author":"Mattei","year":"2006","journal-title":"Eur. J. Cell Biol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"105147","DOI":"10.1016\/j.micinf.2023.105147","article-title":"Extracellular vesicles secreted by Echinococcus multilocularis: Important players in angiogenesis promotion","volume":"25","author":"Liu","year":"2023","journal-title":"Microbes Infect."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1093\/infdis\/159.3.420","article-title":"Entamoeba histolytica: From Adherence to Enteropathy","volume":"159","author":"Ravdin","year":"1989","journal-title":"J. Infect. Dis."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1501","DOI":"10.2217\/fmb.11.120","article-title":"Mechanisms of adherence, cytotoxicity and phagocytosis modulate the pathogenesis of Entamoeba histolytica","volume":"6","author":"Christy","year":"2011","journal-title":"Futur. Microbiol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"125857","DOI":"10.1016\/j.protis.2022.125857","article-title":"External pH Variations Modify Proliferation, Erythrophagocytosis, Cytoskeleton Remodeling, and Cell Morphology of Entamoeba histolytica Trophozoites","volume":"173","year":"2022","journal-title":"Protist"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"S140","DOI":"10.1016\/S0188-4409(00)00133-8","article-title":"The Interplay Between Receptor Capping and Cytoskeleton Remodeling in Entamoeba histolytica","volume":"31","author":"Tavares","year":"2000","journal-title":"Arch. Med. Res."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/j.exppara.2007.01.011","article-title":"Entamoeba histolytica: Apoptosis induced in vitro by nitric oxide species","volume":"116","author":"Ramos","year":"2007","journal-title":"Exp. Parasitol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"640","DOI":"10.1111\/mmi.15061","article-title":"Apoptosis-inducing factor-like protein-mediated stress and metronidazole-responsive programmed cell death pathway in Entamoeba histolytica","volume":"119","author":"Bandyopadhyay","year":"2023","journal-title":"Mol. Microbiol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1016\/j.parint.2010.01.001","article-title":"Hydrogen peroxide-induced apoptosis-like cell death in Entamoeba histolytica","volume":"59","author":"Ghosh","year":"2010","journal-title":"Parasitol. Int."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"1893","DOI":"10.1242\/jcs.00395","article-title":"Bro1 is an endosome-associated protein that functions in the MVB pathway in Saccharomyces cerevisiae","volume":"116","author":"Odorizzi","year":"2003","journal-title":"J. Cell Sci."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"26986","DOI":"10.1038\/srep26986","article-title":"ALG-2 interacting protein-X (Alix) is essential for clathrin-independent endocytosis and signaling","volume":"6","author":"Mercier","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1016\/j.str.2009.04.007","article-title":"A Crescent-Shaped ALIX Dimer Targets ESCRT-III CHMP4 Filaments","volume":"17","author":"Pires","year":"2009","journal-title":"Structure"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1016\/j.devcel.2013.04.003","article-title":"Viral Infection Controlled by a Calcium-Dependent Lipid-Binding Module in ALIX","volume":"25","author":"Bissig","year":"2013","journal-title":"Dev. Cell"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"4660","DOI":"10.1091\/mbc.E15-05-0284","article-title":"The \u03b1-arrestin ARRDC3 mediates ALIX ubiquitination and G protein\u2013coupled receptor lysosomal sorting","volume":"26","author":"Dores","year":"2015","journal-title":"Mol. Biol. Cell"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1038\/nprot.2010.5","article-title":"I-TASSER: A unified platform for automated protein structure and function prediction","volume":"5","author":"Roy","year":"2010","journal-title":"Nat. Protoc."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1016\/0035-9203(78)90144-X","article-title":"A new medium for the axenic cultivation of entamoeba histolytica and other entamoeba","volume":"72","author":"Diamond","year":"1978","journal-title":"Trans. R. Soc. Trop. Med. Hyg."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1083\/jcb.77.3.853","article-title":"Polarized monolayers formed by epithelial cells on a permeable and translucent support","volume":"77","author":"Cereijido","year":"1978","journal-title":"J. Cell Biol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/S0166-6851(96)02771-5","article-title":"Tetracycline-controlled gene expression in Entamoeba histolytica","volume":"84","author":"Hamann","year":"1997","journal-title":"Mol. Biochem. Parasitol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"8975","DOI":"10.1073\/pnas.92.19.8975","article-title":"Transfection and continuous expression of heterologous genes in the protozoan parasite Entamoeba histolytica","volume":"92","author":"Hamann","year":"1995","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.1007\/s00436-020-06621-7","article-title":"Functional characterization and subcellular distribution of two recombinant cytosolic HSP70 isoforms from Entamoeba histolytica under normal and stress conditions","volume":"119","author":"Santos","year":"2020","journal-title":"Parasitol. Res."},{"key":"ref_78","doi-asserted-by":"crossref","unstructured":"Talam\u00e1s-Lara, D., Ch\u00e1vez-Mungu\u00eda, B., Gonz\u00e1lez-Robles, A., Talam\u00e1s-Rohana, P., Salazar-Villatoro, L., Dur\u00e1n-D\u00edaz, \u00c1., and Mart\u00ednez-Palomo, A. (2014). Erythrophagocytosis in Entamoeba histolytica and Entamoeba dispar: A Comparative Study. BioMed Res. Int., 2014.","DOI":"10.1155\/2014\/626259"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"1006","DOI":"10.1177\/20.12.1006","article-title":"Studies on microperoxisomes II. A cytochemical method for light and electron microscopy","volume":"20","author":"Novikoff","year":"1972","journal-title":"J. Histochem. Cytochem."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/25\/14\/7609\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T15:15:10Z","timestamp":1760109310000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/25\/14\/7609"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,7,11]]},"references-count":79,"journal-issue":{"issue":"14","published-online":{"date-parts":[[2024,7]]}},"alternative-id":["ijms25147609"],"URL":"https:\/\/doi.org\/10.3390\/ijms25147609","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,7,11]]}}}