Protein sumoylation is crucial for phagocytosis in entamoeba histolytica trophozoites
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), a...
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Díaz-Hernández, Mitzi Javier-Reyna, Rosario Sotto-Ortega, Izaid José García-Rivera, Guillermina Montaño, Sarita Betanzo, Abigail Zanatta, Dxinegueela Orozco, Esther Ciencia UDES 2022-03-01T15:52:34Z 2022-03-01T15:52:34Z 2021-05-27 Digital 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 ΨKXE/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 ΨKXE/D binding motif. Ciencias Médicas y de la Salud 24 p application/pdf https://doi.org/10.3390/ijms22115709 https://repositorio.udes.edu.co/handle/001/6197 eng Suiza 24 11 1 22 Díaz-Hernández, M.; Javier-Reyna, R.; Sotto-Ortega, I.; García-Rivera, G.; Montaño, S.; Betanzos, A.; Zanatta, D.; Orozco, E. Protein Sumoylation Is Crucial for Phagocytosis in Entamoeba histolytica Trophozoites. Int. J. Mol. Sci. 2021, 22, 5709. https://doi.org/10.3390/ ijms22115709 Scopus International Journal of Molecular Sciences © 2021 by the authors. Licensee MDPI, Basel, Switzerland. info:eu-repo/semantics/openAccess Atribución-NoComercial 4.0 Internacional (CC BY-NC 4.0) https://creativecommons.org/licenses/by-nc/4.0/ https://www.mdpi.com/1422-0067/22/11/5709 SUMOylation Phagocytosis E. histolytica ESCRT machinery EhADH adhesin Protein sumoylation is crucial for phagocytosis in entamoeba histolytica trophozoites Artículo de revista http://purl.org/coar/resource_type/c_6501 Text info:eu-repo/semantics/article http://purl.org/redcol/resource_type/ART info:eu-repo/semantics/publishedVersion Todas las Audiencias Publication http://purl.org/coar/access_right/c_abf2 http://purl.org/coar/version/c_970fb48d4fbd8a85 |
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Universidad EIA |
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d_repositorio.udes.edu.co-DSPACE |
| title |
Protein sumoylation is crucial for phagocytosis in entamoeba histolytica trophozoites |
| spellingShingle |
Protein sumoylation is crucial for phagocytosis in entamoeba histolytica trophozoites Díaz-Hernández, Mitzi Javier-Reyna, Rosario Sotto-Ortega, Izaid José García-Rivera, Guillermina Montaño, Sarita Betanzo, Abigail Zanatta, Dxinegueela Orozco, Esther Díaz-Hernández, Mitzi Javier-Reyna, Rosario Sotto-Ortega, Izaid José García-Rivera, Guillermina Montaño, Sarita Betanzo, Abigail Zanatta, Dxinegueela Orozco, Esther Ciencia UDES SUMOylation Phagocytosis E. histolytica ESCRT machinery EhADH adhesin |
| title_short |
Protein sumoylation is crucial for phagocytosis in entamoeba histolytica trophozoites |
| title_full |
Protein sumoylation is crucial for phagocytosis in entamoeba histolytica trophozoites |
| title_fullStr |
Protein sumoylation is crucial for phagocytosis in entamoeba histolytica trophozoites |
| title_full_unstemmed |
Protein sumoylation is crucial for phagocytosis in entamoeba histolytica trophozoites |
| title_sort |
protein sumoylation is crucial for phagocytosis in entamoeba histolytica trophozoites |
| author |
Díaz-Hernández, Mitzi Javier-Reyna, Rosario Sotto-Ortega, Izaid José García-Rivera, Guillermina Montaño, Sarita Betanzo, Abigail Zanatta, Dxinegueela Orozco, Esther Díaz-Hernández, Mitzi Javier-Reyna, Rosario Sotto-Ortega, Izaid José García-Rivera, Guillermina Montaño, Sarita Betanzo, Abigail Zanatta, Dxinegueela Orozco, Esther Ciencia UDES |
| author_facet |
Díaz-Hernández, Mitzi Javier-Reyna, Rosario Sotto-Ortega, Izaid José García-Rivera, Guillermina Montaño, Sarita Betanzo, Abigail Zanatta, Dxinegueela Orozco, Esther Díaz-Hernández, Mitzi Javier-Reyna, Rosario Sotto-Ortega, Izaid José García-Rivera, Guillermina Montaño, Sarita Betanzo, Abigail Zanatta, Dxinegueela Orozco, Esther Ciencia UDES |
| building |
Repositorio digital |
| topic |
SUMOylation Phagocytosis E. histolytica ESCRT machinery EhADH adhesin |
| topic_facet |
SUMOylation Phagocytosis E. histolytica ESCRT machinery EhADH adhesin |
| publishDate |
2021-05-27 |
| language |
English |
| publisher |
Suiza |
| physical |
24 p |
| format |
Artículo de revista |
| description |
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 ΨKXE/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 ΨKXE/D binding motif.
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| url |
https://repositorio.udes.edu.co/handle/001/6197 |
| url_str_mv |
https://repositorio.udes.edu.co/handle/001/6197 |
| _version_ |
1789501968203382784 |
| score |
11.25946 |
