Brothers in Arms: Structure, Assembly and Function of <i>Arenaviridae</i> Nucleoprotein
<i>Arenaviridae</i> is a family of viruses harbouring important emerging pathogens belonging to the <i>Bunyavirales</i> order. Like in other segmented negative strand RNA viruses, the nucleoprotein (NP) is a major actor of the viral life cycle being both (i) the necessary co-...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-07-01
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| Series: | Viruses |
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| Online Access: | https://www.mdpi.com/1999-4915/12/7/772 |
| _version_ | 1827712920404885504 |
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| author | Nicolas Papageorgiou Maria Spiliopoulou Thi-Hong Van Nguyen Afroditi Vaitsopoulou Elsie Yekwa Laban Karine Alvarez Irene Margiolaki Bruno Canard François Ferron |
| author_facet | Nicolas Papageorgiou Maria Spiliopoulou Thi-Hong Van Nguyen Afroditi Vaitsopoulou Elsie Yekwa Laban Karine Alvarez Irene Margiolaki Bruno Canard François Ferron |
| author_sort | Nicolas Papageorgiou |
| collection | DOAJ |
| description | <i>Arenaviridae</i> is a family of viruses harbouring important emerging pathogens belonging to the <i>Bunyavirales</i> order. Like in other segmented negative strand RNA viruses, the nucleoprotein (NP) is a major actor of the viral life cycle being both (i) the necessary co-factor of the polymerase present in the L protein, and (ii) the last line of defence of the viral genome (vRNA) by physically hiding its presence in the cytoplasm. The NP is also one of the major players interfering with the immune system. Several structural studies of NP have shown that it features two domains: a globular RNA binding domain (NP-core) in its N-terminal and an exonuclease domain (ExoN) in its C-terminal. Further studies have observed that significant conformational changes are necessary for RNA encapsidation. In this review we revisited the most recent structural and functional data available on <i>Arenaviridae</i> NP, compared to other <i>Bunyavirales</i> nucleoproteins and explored the structural and functional implications. We review the variety of structural motif extensions involved in NP–NP binding mode. We also evaluate the major functional implications of NP interactome and the role of ExoN, thus making the NP a target of choice for future vaccine and antiviral therapy. |
| first_indexed | 2024-03-10T18:25:01Z |
| format | Article |
| id | doaj.art-be3e1ee0e2b44ddc80f928f3c1892973 |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-03-10T18:25:01Z |
| publishDate | 2020-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-be3e1ee0e2b44ddc80f928f3c18929732023-11-20T07:05:49ZengMDPI AGViruses1999-49152020-07-0112777210.3390/v12070772Brothers in Arms: Structure, Assembly and Function of <i>Arenaviridae</i> NucleoproteinNicolas Papageorgiou0Maria Spiliopoulou1Thi-Hong Van Nguyen2Afroditi Vaitsopoulou3Elsie Yekwa Laban4Karine Alvarez5Irene Margiolaki6Bruno Canard7François Ferron8Architecture et Fonction des Macromolécules Biologiques, CNRS - UMR 7257, Polytech Case 925, 13009 Marseille, FranceSection of Genetics, Cell Biology and Development, Department of Biology, University of Patras, GR-26500 Patras, Greece Patras, GreeceArchitecture et Fonction des Macromolécules Biologiques, CNRS - UMR 7257, Polytech Case 925, 13009 Marseille, FranceAix-Marseille Université, AFMB UMR 7257, 13288 Marseille, FranceArchitecture et Fonction des Macromolécules Biologiques, CNRS - UMR 7257, Polytech Case 925, 13009 Marseille, FranceArchitecture et Fonction des Macromolécules Biologiques, CNRS - UMR 7257, Polytech Case 925, 13009 Marseille, FranceSection of Genetics, Cell Biology and Development, Department of Biology, University of Patras, GR-26500 Patras, Greece Patras, GreeceArchitecture et Fonction des Macromolécules Biologiques, CNRS - UMR 7257, Polytech Case 925, 13009 Marseille, FranceArchitecture et Fonction des Macromolécules Biologiques, CNRS - UMR 7257, Polytech Case 925, 13009 Marseille, France<i>Arenaviridae</i> is a family of viruses harbouring important emerging pathogens belonging to the <i>Bunyavirales</i> order. Like in other segmented negative strand RNA viruses, the nucleoprotein (NP) is a major actor of the viral life cycle being both (i) the necessary co-factor of the polymerase present in the L protein, and (ii) the last line of defence of the viral genome (vRNA) by physically hiding its presence in the cytoplasm. The NP is also one of the major players interfering with the immune system. Several structural studies of NP have shown that it features two domains: a globular RNA binding domain (NP-core) in its N-terminal and an exonuclease domain (ExoN) in its C-terminal. Further studies have observed that significant conformational changes are necessary for RNA encapsidation. In this review we revisited the most recent structural and functional data available on <i>Arenaviridae</i> NP, compared to other <i>Bunyavirales</i> nucleoproteins and explored the structural and functional implications. We review the variety of structural motif extensions involved in NP–NP binding mode. We also evaluate the major functional implications of NP interactome and the role of ExoN, thus making the NP a target of choice for future vaccine and antiviral therapy.https://www.mdpi.com/1999-4915/12/7/772<i>Arenaviridae</i><i>Bunyavirales</i>emerging diseasesexonucleasenucleoproteinstructure |
| spellingShingle | Nicolas Papageorgiou Maria Spiliopoulou Thi-Hong Van Nguyen Afroditi Vaitsopoulou Elsie Yekwa Laban Karine Alvarez Irene Margiolaki Bruno Canard François Ferron Brothers in Arms: Structure, Assembly and Function of <i>Arenaviridae</i> Nucleoprotein Viruses <i>Arenaviridae</i> <i>Bunyavirales</i> emerging diseases exonuclease nucleoprotein structure |
| title | Brothers in Arms: Structure, Assembly and Function of <i>Arenaviridae</i> Nucleoprotein |
| title_full | Brothers in Arms: Structure, Assembly and Function of <i>Arenaviridae</i> Nucleoprotein |
| title_fullStr | Brothers in Arms: Structure, Assembly and Function of <i>Arenaviridae</i> Nucleoprotein |
| title_full_unstemmed | Brothers in Arms: Structure, Assembly and Function of <i>Arenaviridae</i> Nucleoprotein |
| title_short | Brothers in Arms: Structure, Assembly and Function of <i>Arenaviridae</i> Nucleoprotein |
| title_sort | brothers in arms structure assembly and function of i arenaviridae i nucleoprotein |
| topic | <i>Arenaviridae</i> <i>Bunyavirales</i> emerging diseases exonuclease nucleoprotein structure |
| url | https://www.mdpi.com/1999-4915/12/7/772 |
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