TRIM2, a novel member of the antiviral family, limits New World arenavirus entry
Editor(es): Rajsbaum, R.
Resumen:
Tripartite motif (TRIM) proteins belong to a large family with many roles in host biology, including restricting virus infection. Here, we found that TRIM2, which has been implicated in cases of Charcot–Marie–Tooth disease (CMTD) in humans, acts by blocking hemorrhagic fever New World arenavirus (NWA) entry into cells. We show that Trim2-knockout mice, as well as primary fibroblasts from a CMTD patient with mutations in TRIM2, are more highly infected by the NWAs Junı´n and Tacaribe virus than wild-type mice or cells are. Using mice with different Trim2 gene deletions and TRIM2 mutant constructs, we demonstrate that its antiviral activity is uniquely independent of the RING domain encoding ubiquitin ligase activity. Finally, we show that one member of the TRIM2 interactome, signal regulatory protein α (SIRPA), a known inhibitor of phagocytosis, also restricts NWA infection and conversely that TRIM2 limits phagocytosis of apoptotic cells. In addition to demonstrating a novel antiviral mechanism for TRIM proteins, these studies suggest that the NWA entry and phagocytosis pathways overlap
| 2019 | |
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Tripartite motif (TRIM) New World arenaviruses Virus infection |
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| Inglés | |
| Universidad de la República | |
| COLIBRI | |
| https://hdl.handle.net/20.500.12008/28105 | |
| Acceso abierto | |
| Licencia Creative Commons Atribución (CC - By 4.0) |
| _version_ | 1807522786157002752 |
|---|---|
| author | Sarute, Nicolás |
| author2 | Ibrahim, N. Medegan Fagla, B. Lavanya, M. Cuevas, C. Stavrou, S. Otkiran-Clare, G. Tyynismaa, H. Henao-Mejia, J. Ross, S. R. |
| author2_role | author author author author author author author author author |
| author_facet | Sarute, Nicolás Ibrahim, N. Medegan Fagla, B. Lavanya, M. Cuevas, C. Stavrou, S. Otkiran-Clare, G. Tyynismaa, H. Henao-Mejia, J. Ross, S. R. |
| author_role | author |
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| collection | COLIBRI |
| dc.contributor.filiacion.none.fl_str_mv | Sarute Nicolás, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología. Ibrahim N. Medegan Fagla B. Lavanya M. Cuevas C. Stavrou S. Otkiran-Clare G. Tyynismaa H. Henao-Mejia J. Ross S.R. |
| dc.creator.editor.none.fl_str_mv | Rajsbaum, R. |
| dc.creator.none.fl_str_mv | Sarute, Nicolás Ibrahim, N. Medegan Fagla, B. Lavanya, M. Cuevas, C. Stavrou, S. Otkiran-Clare, G. Tyynismaa, H. Henao-Mejia, J. Ross, S. R. |
| dc.date.accessioned.none.fl_str_mv | 2021-06-08T13:37:55Z |
| dc.date.available.none.fl_str_mv | 2021-06-08T13:37:55Z |
| dc.date.issued.none.fl_str_mv | 2019 |
| dc.description.abstract.none.fl_txt_mv | Tripartite motif (TRIM) proteins belong to a large family with many roles in host biology, including restricting virus infection. Here, we found that TRIM2, which has been implicated in cases of Charcot–Marie–Tooth disease (CMTD) in humans, acts by blocking hemorrhagic fever New World arenavirus (NWA) entry into cells. We show that Trim2-knockout mice, as well as primary fibroblasts from a CMTD patient with mutations in TRIM2, are more highly infected by the NWAs Junı´n and Tacaribe virus than wild-type mice or cells are. Using mice with different Trim2 gene deletions and TRIM2 mutant constructs, we demonstrate that its antiviral activity is uniquely independent of the RING domain encoding ubiquitin ligase activity. Finally, we show that one member of the TRIM2 interactome, signal regulatory protein α (SIRPA), a known inhibitor of phagocytosis, also restricts NWA infection and conversely that TRIM2 limits phagocytosis of apoptotic cells. In addition to demonstrating a novel antiviral mechanism for TRIM proteins, these studies suggest that the NWA entry and phagocytosis pathways overlap |
| dc.format.extent.es.fl_str_mv | 26 h. |
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| dc.identifier.citation.es.fl_str_mv | Sarute, N, Ibrahim, N, Medegan Fagla, B, [y otros] "TRIM2, a novel member of the antiviral family, limits New World arenavirus entry". PLoS Biology. [en línea] 2019, 17(2): e3000137. 26 h. DOI: 10.1371/journal.pbio.3000137 |
| dc.identifier.doi.none.fl_str_mv | 10.1371/journal.pbio.3000137 |
| dc.identifier.issn.none.fl_str_mv | 1545-7885 |
| dc.identifier.uri.none.fl_str_mv | https://hdl.handle.net/20.500.12008/28105 |
| dc.language.iso.none.fl_str_mv | en eng |
| dc.publisher.es.fl_str_mv | Public Library of Science |
| dc.relation.ispartof.es.fl_str_mv | PLoS Biology, 2019, 17(2): e3000137 |
| dc.rights.license.none.fl_str_mv | Licencia Creative Commons Atribución (CC - By 4.0) |
| dc.rights.none.fl_str_mv | info:eu-repo/semantics/openAccess |
| dc.source.none.fl_str_mv | reponame:COLIBRI instname:Universidad de la República instacron:Universidad de la República |
| dc.subject.es.fl_str_mv | Tripartite motif (TRIM) New World arenaviruses Virus infection |
| dc.title.none.fl_str_mv | TRIM2, a novel member of the antiviral family, limits New World arenavirus entry |
| dc.type.es.fl_str_mv | Artículo |
| dc.type.none.fl_str_mv | info:eu-repo/semantics/article |
| dc.type.version.none.fl_str_mv | info:eu-repo/semantics/publishedVersion |
| description | Tripartite motif (TRIM) proteins belong to a large family with many roles in host biology, including restricting virus infection. Here, we found that TRIM2, which has been implicated in cases of Charcot–Marie–Tooth disease (CMTD) in humans, acts by blocking hemorrhagic fever New World arenavirus (NWA) entry into cells. We show that Trim2-knockout mice, as well as primary fibroblasts from a CMTD patient with mutations in TRIM2, are more highly infected by the NWAs Junı´n and Tacaribe virus than wild-type mice or cells are. Using mice with different Trim2 gene deletions and TRIM2 mutant constructs, we demonstrate that its antiviral activity is uniquely independent of the RING domain encoding ubiquitin ligase activity. Finally, we show that one member of the TRIM2 interactome, signal regulatory protein α (SIRPA), a known inhibitor of phagocytosis, also restricts NWA infection and conversely that TRIM2 limits phagocytosis of apoptotic cells. In addition to demonstrating a novel antiviral mechanism for TRIM proteins, these studies suggest that the NWA entry and phagocytosis pathways overlap |
| eu_rights_str_mv | openAccess |
| format | article |
| id | COLIBRI_aa79840b4c91fe0388911833de2f1e5c |
| identifier_str_mv | Sarute, N, Ibrahim, N, Medegan Fagla, B, [y otros] "TRIM2, a novel member of the antiviral family, limits New World arenavirus entry". PLoS Biology. [en línea] 2019, 17(2): e3000137. 26 h. DOI: 10.1371/journal.pbio.3000137 1545-7885 10.1371/journal.pbio.3000137 |
| instacron_str | Universidad de la República |
| institution | Universidad de la República |
| instname_str | Universidad de la República |
| language | eng |
| language_invalid_str_mv | en |
| network_acronym_str | COLIBRI |
| network_name_str | COLIBRI |
| oai_identifier_str | oai:colibri.udelar.edu.uy:20.500.12008/28105 |
| publishDate | 2019 |
| reponame_str | COLIBRI |
| repository.mail.fl_str_mv | mabel.seroubian@seciu.edu.uy |
| repository.name.fl_str_mv | COLIBRI - Universidad de la República |
| repository_id_str | 4771 |
| rights_invalid_str_mv | Licencia Creative Commons Atribución (CC - By 4.0) |
| spelling | Sarute Nicolás, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología.Ibrahim N.Medegan Fagla B.Lavanya M.Cuevas C.Stavrou S.Otkiran-Clare G.Tyynismaa H.Henao-Mejia J.Ross S.R.2021-06-08T13:37:55Z2021-06-08T13:37:55Z2019Sarute, N, Ibrahim, N, Medegan Fagla, B, [y otros] "TRIM2, a novel member of the antiviral family, limits New World arenavirus entry". PLoS Biology. [en línea] 2019, 17(2): e3000137. 26 h. DOI: 10.1371/journal.pbio.30001371545-7885https://hdl.handle.net/20.500.12008/2810510.1371/journal.pbio.3000137Tripartite motif (TRIM) proteins belong to a large family with many roles in host biology, including restricting virus infection. Here, we found that TRIM2, which has been implicated in cases of Charcot–Marie–Tooth disease (CMTD) in humans, acts by blocking hemorrhagic fever New World arenavirus (NWA) entry into cells. We show that Trim2-knockout mice, as well as primary fibroblasts from a CMTD patient with mutations in TRIM2, are more highly infected by the NWAs Junı´n and Tacaribe virus than wild-type mice or cells are. Using mice with different Trim2 gene deletions and TRIM2 mutant constructs, we demonstrate that its antiviral activity is uniquely independent of the RING domain encoding ubiquitin ligase activity. Finally, we show that one member of the TRIM2 interactome, signal regulatory protein α (SIRPA), a known inhibitor of phagocytosis, also restricts NWA infection and conversely that TRIM2 limits phagocytosis of apoptotic cells. In addition to demonstrating a novel antiviral mechanism for TRIM proteins, these studies suggest that the NWA entry and phagocytosis pathways overlapSubmitted by Verdun Juan Pablo (jverdun@fcien.edu.uy) on 2021-06-07T22:42:35Z No. of bitstreams: 2 license_rdf: 19875 bytes, checksum: 9fdbed07f52437945402c4e70fa4773e (MD5) 10.1371journal.pbio.3000137.pdf: 3188078 bytes, checksum: 23c1f59c2b16aed472bca824fea55358 (MD5)Approved for entry into archive by Faget Cecilia (lfaget@fcien.edu.uy) on 2021-06-08T12:42:09Z (GMT) No. of bitstreams: 2 license_rdf: 19875 bytes, checksum: 9fdbed07f52437945402c4e70fa4773e (MD5) 10.1371journal.pbio.3000137.pdf: 3188078 bytes, checksum: 23c1f59c2b16aed472bca824fea55358 (MD5)Made available in DSpace by Luna Fabiana (fabiana.luna@seciu.edu.uy) on 2021-06-08T13:37:55Z (GMT). No. of bitstreams: 2 license_rdf: 19875 bytes, checksum: 9fdbed07f52437945402c4e70fa4773e (MD5) 10.1371journal.pbio.3000137.pdf: 3188078 bytes, checksum: 23c1f59c2b16aed472bca824fea55358 (MD5) Previous issue date: 201926 h.application/pdfenengPublic Library of SciencePLoS Biology, 2019, 17(2): e3000137Las obras depositadas en el Repositorio se rigen por la Ordenanza de los Derechos de la Propiedad Intelectual de la Universidad de la República.(Res. Nº 91 de C.D.C. de 8/III/1994 – D.O. 7/IV/1994) y por la Ordenanza del Repositorio Abierto de la Universidad de la República (Res. Nº 16 de C.D.C. de 07/10/2014)info:eu-repo/semantics/openAccessLicencia Creative Commons Atribución (CC - By 4.0)Tripartite motif (TRIM)New World arenavirusesVirus infectionTRIM2, a novel member of the antiviral family, limits New World arenavirus entryArtículoinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionreponame:COLIBRIinstname:Universidad de la Repúblicainstacron:Universidad de la RepúblicaSarute, NicolásIbrahim, N.Medegan Fagla, B.Lavanya, M.Cuevas, C.Stavrou, S.Otkiran-Clare, G.Tyynismaa, H.Henao-Mejia, J.Ross, S. 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- Universidad de la Repúblicafalse |
| spellingShingle | TRIM2, a novel member of the antiviral family, limits New World arenavirus entry Sarute, Nicolás Tripartite motif (TRIM) New World arenaviruses Virus infection |
| status_str | publishedVersion |
| title | TRIM2, a novel member of the antiviral family, limits New World arenavirus entry |
| title_full | TRIM2, a novel member of the antiviral family, limits New World arenavirus entry |
| title_fullStr | TRIM2, a novel member of the antiviral family, limits New World arenavirus entry |
| title_full_unstemmed | TRIM2, a novel member of the antiviral family, limits New World arenavirus entry |
| title_short | TRIM2, a novel member of the antiviral family, limits New World arenavirus entry |
| title_sort | TRIM2, a novel member of the antiviral family, limits New World arenavirus entry |
| topic | Tripartite motif (TRIM) New World arenaviruses Virus infection |
| url | https://hdl.handle.net/20.500.12008/28105 |
