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Brothers in Arms: Structure, Assembly and Function of Arenaviridae Nucleoprotein

Arenaviridae is a family of viruses harbouring important emerging pathogens belonging to the Bunyavirales 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 th...

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Autores principales: Papageorgiou, Nicolas, Spiliopoulou, Maria, Nguyen, Thi-Hong Van, Vaitsopoulou, Afroditi, Laban, Elsie Yekwa, Alvarez, Karine, Margiolaki, Irene, Canard, Bruno, Ferron, François
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7411964/
https://www.ncbi.nlm.nih.gov/pubmed/32708976
http://dx.doi.org/10.3390/v12070772
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author Papageorgiou, Nicolas
Spiliopoulou, Maria
Nguyen, Thi-Hong Van
Vaitsopoulou, Afroditi
Laban, Elsie Yekwa
Alvarez, Karine
Margiolaki, Irene
Canard, Bruno
Ferron, François
author_facet Papageorgiou, Nicolas
Spiliopoulou, Maria
Nguyen, Thi-Hong Van
Vaitsopoulou, Afroditi
Laban, Elsie Yekwa
Alvarez, Karine
Margiolaki, Irene
Canard, Bruno
Ferron, François
author_sort Papageorgiou, Nicolas
collection PubMed
description Arenaviridae is a family of viruses harbouring important emerging pathogens belonging to the Bunyavirales 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 Arenaviridae NP, compared to other Bunyavirales 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.
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spelling pubmed-74119642020-08-25 Brothers in Arms: Structure, Assembly and Function of Arenaviridae Nucleoprotein Papageorgiou, Nicolas Spiliopoulou, Maria Nguyen, Thi-Hong Van Vaitsopoulou, Afroditi Laban, Elsie Yekwa Alvarez, Karine Margiolaki, Irene Canard, Bruno Ferron, François Viruses Review Arenaviridae is a family of viruses harbouring important emerging pathogens belonging to the Bunyavirales 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 Arenaviridae NP, compared to other Bunyavirales 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. MDPI 2020-07-17 /pmc/articles/PMC7411964/ /pubmed/32708976 http://dx.doi.org/10.3390/v12070772 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Papageorgiou, Nicolas
Spiliopoulou, Maria
Nguyen, Thi-Hong Van
Vaitsopoulou, Afroditi
Laban, Elsie Yekwa
Alvarez, Karine
Margiolaki, Irene
Canard, Bruno
Ferron, François
Brothers in Arms: Structure, Assembly and Function of Arenaviridae Nucleoprotein
title Brothers in Arms: Structure, Assembly and Function of Arenaviridae Nucleoprotein
title_full Brothers in Arms: Structure, Assembly and Function of Arenaviridae Nucleoprotein
title_fullStr Brothers in Arms: Structure, Assembly and Function of Arenaviridae Nucleoprotein
title_full_unstemmed Brothers in Arms: Structure, Assembly and Function of Arenaviridae Nucleoprotein
title_short Brothers in Arms: Structure, Assembly and Function of Arenaviridae Nucleoprotein
title_sort brothers in arms: structure, assembly and function of arenaviridae nucleoprotein
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7411964/
https://www.ncbi.nlm.nih.gov/pubmed/32708976
http://dx.doi.org/10.3390/v12070772
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