{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,27]],"date-time":"2026-04-27T23:28:40Z","timestamp":1777332520362,"version":"3.51.4"},"reference-count":72,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2021,5,27]],"date-time":"2021-05-27T00:00:00Z","timestamp":1622073600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003141","name":"Consejo Nacional de Ciencia y Tecnolog\u00eda","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>Posttranslational modifications provide Entamoeba histolytica proteins the timing and signaling to intervene during different processes, such as phagocytosis. However, SUMOylation has not been studied in E. histolytica yet. Here, we characterized the E. histolytica SUMO gene, its product (EhSUMO), and the relevance of SUMOylation in phagocytosis. Our results indicated that EhSUMO has an extended N-terminus that differentiates SUMO from ubiquitin. It also presents the GG residues at the C-terminus and the \u03a8KXE\/D binding motif, both involved in target protein contact. Additionally, the E. histolytica genome possesses the enzymes belonging to the SUMOylation-deSUMOylation machinery. Confocal microscopy assays disclosed a remarkable EhSUMO membrane activity with convoluted and changing structures in trophozoites during erythrophagocytosis. SUMOylated proteins appeared in pseudopodia, phagocytic channels, and around the adhered and ingested erythrocytes. Docking analysis predicted interaction of EhSUMO with EhADH (an ALIX family protein), and immunoprecipitation and immunofluorescence assays revealed that the association increased during phagocytosis; whereas the EhVps32 (a protein of the ESCRT-III complex)-EhSUMO interaction appeared stronger since basal conditions. In EhSUMO knocked-down trophozoites, the bizarre membranous structures disappeared, and EhSUMO interaction with EhADH and EhVps32 diminished. Our results evidenced the presence of a SUMO gene in E. histolytica and the SUMOylation relevance during phagocytosis. This is supported by bioinformatics screening of many other proteins of E. histolytica involved in phagocytosis, which present putative SUMOylation sites and the \u03a8KXE\/D binding motif.<\/jats:p>","DOI":"10.3390\/ijms22115709","type":"journal-article","created":{"date-parts":[[2021,5,27]],"date-time":"2021-05-27T11:07:02Z","timestamp":1622113622000},"page":"5709","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Protein Sumoylation Is Crucial for Phagocytosis in Entamoeba histolytica Trophozoites"],"prefix":"10.3390","volume":"22","author":[{"given":"Mitzi","family":"D\u00edaz-Hern\u00e1ndez","sequence":"first","affiliation":[{"name":"Departamento de Infect\u00f3mica y Patog\u00e9nesis Molecular, Centro de Investigaci\u00f3n y de Estudios Avanzados del IPN, Mexico City 07360, Mexico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rosario","family":"Javier-Reyna","sequence":"additional","affiliation":[{"name":"Departamento de Infect\u00f3mica y Patog\u00e9nesis Molecular, Centro de Investigaci\u00f3n y de Estudios Avanzados del IPN, Mexico City 07360, Mexico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Izaid","family":"Sotto-Ortega","sequence":"additional","affiliation":[{"name":"Bacteriolog\u00eda y Laboratorio Cl\u00ednico, Universidad de Santander, 200004 Valledupar, Colombia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Guillermina","family":"Garc\u00eda-Rivera","sequence":"additional","affiliation":[{"name":"Departamento de Infect\u00f3mica y Patog\u00e9nesis Molecular, Centro de Investigaci\u00f3n y de Estudios Avanzados del IPN, Mexico City 07360, 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":"Laboratorio de Bioinform\u00e1tica y Simulaci\u00f3n Molecular, Facultad de Ciencias Qu\u00edmico Biol\u00f3gicas, Universidad Aut\u00f3noma de Sinaloa, Sinaloa 80030, 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":"Departamento de Infect\u00f3mica y Patog\u00e9nesis Molecular, Centro de Investigaci\u00f3n y de Estudios Avanzados del IPN, Mexico City 07360, Mexico"},{"name":"Consejo Nacional de Ciencia y Tecnolog\u00eda (Conacyt), Mexico City 03940, Mexico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dxinegueela","family":"Zanatta","sequence":"additional","affiliation":[{"name":"Departamento de Infect\u00f3mica y Patog\u00e9nesis Molecular, Centro de Investigaci\u00f3n y de Estudios Avanzados del IPN, Mexico City 07360, Mexico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Esther","family":"Orozco","sequence":"additional","affiliation":[{"name":"Departamento de Infect\u00f3mica y Patog\u00e9nesis Molecular, Centro de Investigaci\u00f3n y de Estudios Avanzados del IPN, Mexico City 07360, Mexico"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2021,5,27]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1006\/jmbi.1998.1839","article-title":"Structure determination of the small ubiquitin-related modifier SUMO-1","volume":"280","author":"Bayer","year":"1998","journal-title":"J. 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