EhVps23: A Component of ESCRT-I That Participates in Vesicular Trafficking and Phagocytosis of Entamoeba histolytica
The endosomal sorting complex required for transport (ESCRT) is formed by ESCRT-0, ESCRT-I, ESCRT-II, ESCRT-III complexes, and accessory proteins. It conducts vesicular trafficking in eukaryotes through the formation of vesicles and membrane fission and fusion events. The trophozoites of Entamoeba h...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2021-10-01
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| Series: | Frontiers in Cellular and Infection Microbiology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fcimb.2021.770759/full |
| _version_ | 1818574335213830144 |
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| author | Ausencio Galindo Rosario Javier-Reyna Guillermina García-Rivera Cecilia Bañuelos Sarita Montaño Jaime Ortega-Lopez Bibiana Chávez-Munguía Lizbeth Salazar-Villatoro Esther Orozco |
| author_facet | Ausencio Galindo Rosario Javier-Reyna Guillermina García-Rivera Cecilia Bañuelos Sarita Montaño Jaime Ortega-Lopez Bibiana Chávez-Munguía Lizbeth Salazar-Villatoro Esther Orozco |
| author_sort | Ausencio Galindo |
| collection | DOAJ |
| description | The endosomal sorting complex required for transport (ESCRT) is formed by ESCRT-0, ESCRT-I, ESCRT-II, ESCRT-III complexes, and accessory proteins. It conducts vesicular trafficking in eukaryotes through the formation of vesicles and membrane fission and fusion events. The trophozoites of Entamoeba histolytica, the protozoan responsible for human amoebiasis, presents an active membrane movement in basal state that increases during phagocytosis and tissue invasion. ESCRT-III complex has a pivotal role during these events, but ESCRT-0, ESCRT-I and ESCRT-II have been poorly studied. Here, we unveiled the E. histolytica ESCRT-I complex and its implication in vesicular trafficking and phagocytosis, as well as the molecular relationships with other phagocytosis-involved molecules. We found a gene encoding for a putative EhVps23 protein with the ubiquitin-binding and Vps23 core domains. In basal state, it was in the plasma membrane, cytoplasmic vesicles and multivesicular bodies, whereas during phagocytosis it was extensively ubiquitinated and detected in phagosomes and connected vesicles. Docking analysis, immunoprecipitation assays and microscopy studies evidenced its interaction with EhUbiquitin, EhADH, EhVps32 proteins, and the lysobisphosphatidic acid phospholipid. The knocking down of the Ehvps23 gene resulted in lower rates of phagocytosis. Our results disclosed the concert of finely regulated molecules and vesicular structures participating in vesicular trafficking-related events with a pivotal role of EhVps23. |
| first_indexed | 2024-12-15T00:25:14Z |
| format | Article |
| id | doaj.art-b4e741feae734c6aaa99a103b1b17697 |
| institution | Directory Open Access Journal |
| issn | 2235-2988 |
| language | English |
| last_indexed | 2024-12-15T00:25:14Z |
| publishDate | 2021-10-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Cellular and Infection Microbiology |
| spelling | doaj.art-b4e741feae734c6aaa99a103b1b176972022-12-21T22:42:12ZengFrontiers Media S.A.Frontiers in Cellular and Infection Microbiology2235-29882021-10-011110.3389/fcimb.2021.770759770759EhVps23: A Component of ESCRT-I That Participates in Vesicular Trafficking and Phagocytosis of Entamoeba histolyticaAusencio Galindo0Rosario Javier-Reyna1Guillermina García-Rivera2Cecilia Bañuelos3Sarita Montaño4Jaime Ortega-Lopez5Bibiana Chávez-Munguía6Lizbeth Salazar-Villatoro7Esther Orozco8Departamento de Infectómica y Patogénesis Molecular, Centro de Investigación y de Estudios Avanzados del IPN, Ciudad de México, MexicoDepartamento de Infectómica y Patogénesis Molecular, Centro de Investigación y de Estudios Avanzados del IPN, Ciudad de México, MexicoDepartamento de Infectómica y Patogénesis Molecular, Centro de Investigación y de Estudios Avanzados del IPN, Ciudad de México, MexicoPrograma Transdisciplinario en Desarrollo Científico y Tecnológico para la Sociedad, Centro de Investigación y de Estudios Avanzados del IPN, Ciudad de México, MexicoLaboratorio de Bioinformática y Simulación Molecular, Facultad de Ciencias Químico-Biológicas, Universidad Autónoma de Sinaloa, Sinaloa, MexicoDepartamento de Biotecnología y Bioingeniería, Centro de Investigación y de Estudios Avanzados del IPN, Ciudad de México, MexicoDepartamento de Infectómica y Patogénesis Molecular, Centro de Investigación y de Estudios Avanzados del IPN, Ciudad de México, MexicoDepartamento de Infectómica y Patogénesis Molecular, Centro de Investigación y de Estudios Avanzados del IPN, Ciudad de México, MexicoDepartamento de Infectómica y Patogénesis Molecular, Centro de Investigación y de Estudios Avanzados del IPN, Ciudad de México, MexicoThe endosomal sorting complex required for transport (ESCRT) is formed by ESCRT-0, ESCRT-I, ESCRT-II, ESCRT-III complexes, and accessory proteins. It conducts vesicular trafficking in eukaryotes through the formation of vesicles and membrane fission and fusion events. The trophozoites of Entamoeba histolytica, the protozoan responsible for human amoebiasis, presents an active membrane movement in basal state that increases during phagocytosis and tissue invasion. ESCRT-III complex has a pivotal role during these events, but ESCRT-0, ESCRT-I and ESCRT-II have been poorly studied. Here, we unveiled the E. histolytica ESCRT-I complex and its implication in vesicular trafficking and phagocytosis, as well as the molecular relationships with other phagocytosis-involved molecules. We found a gene encoding for a putative EhVps23 protein with the ubiquitin-binding and Vps23 core domains. In basal state, it was in the plasma membrane, cytoplasmic vesicles and multivesicular bodies, whereas during phagocytosis it was extensively ubiquitinated and detected in phagosomes and connected vesicles. Docking analysis, immunoprecipitation assays and microscopy studies evidenced its interaction with EhUbiquitin, EhADH, EhVps32 proteins, and the lysobisphosphatidic acid phospholipid. The knocking down of the Ehvps23 gene resulted in lower rates of phagocytosis. Our results disclosed the concert of finely regulated molecules and vesicular structures participating in vesicular trafficking-related events with a pivotal role of EhVps23.https://www.frontiersin.org/articles/10.3389/fcimb.2021.770759/fullvesicular traffickingEntamoeba histolyticaESCRTphagocytosisEhVps23 |
| spellingShingle | Ausencio Galindo Rosario Javier-Reyna Guillermina García-Rivera Cecilia Bañuelos Sarita Montaño Jaime Ortega-Lopez Bibiana Chávez-Munguía Lizbeth Salazar-Villatoro Esther Orozco EhVps23: A Component of ESCRT-I That Participates in Vesicular Trafficking and Phagocytosis of Entamoeba histolytica Frontiers in Cellular and Infection Microbiology vesicular trafficking Entamoeba histolytica ESCRT phagocytosis EhVps23 |
| title | EhVps23: A Component of ESCRT-I That Participates in Vesicular Trafficking and Phagocytosis of Entamoeba histolytica |
| title_full | EhVps23: A Component of ESCRT-I That Participates in Vesicular Trafficking and Phagocytosis of Entamoeba histolytica |
| title_fullStr | EhVps23: A Component of ESCRT-I That Participates in Vesicular Trafficking and Phagocytosis of Entamoeba histolytica |
| title_full_unstemmed | EhVps23: A Component of ESCRT-I That Participates in Vesicular Trafficking and Phagocytosis of Entamoeba histolytica |
| title_short | EhVps23: A Component of ESCRT-I That Participates in Vesicular Trafficking and Phagocytosis of Entamoeba histolytica |
| title_sort | ehvps23 a component of escrt i that participates in vesicular trafficking and phagocytosis of entamoeba histolytica |
| topic | vesicular trafficking Entamoeba histolytica ESCRT phagocytosis EhVps23 |
| url | https://www.frontiersin.org/articles/10.3389/fcimb.2021.770759/full |
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