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Biophysical characterisation of the nucleocapsid protein from a highly pathogenic porcine reproductive and respiratory syndrome virus strain

The arterivirus nucleocapsid (N) protein is a multifunctional protein that binds viral RNA for encapsidation and has potential roles in host cell processes. This study characterised the N protein from a highly virulent North American strain of porcine reproductive and respiratory syndrome virus (PRR...

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Detalles Bibliográficos
Autores principales: Jourdan, Stefanie S., Osorio, Fernando A., Hiscox, Julian A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Inc. 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7092862/
https://www.ncbi.nlm.nih.gov/pubmed/22306009
http://dx.doi.org/10.1016/j.bbrc.2011.11.126
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author Jourdan, Stefanie S.
Osorio, Fernando A.
Hiscox, Julian A.
author_facet Jourdan, Stefanie S.
Osorio, Fernando A.
Hiscox, Julian A.
author_sort Jourdan, Stefanie S.
collection PubMed
description The arterivirus nucleocapsid (N) protein is a multifunctional protein that binds viral RNA for encapsidation and has potential roles in host cell processes. This study characterised the N protein from a highly virulent North American strain of porcine reproductive and respiratory syndrome virus (PRRSV). The association with viral RNA was mapped to defined motifs on the N protein. The results indicated that disulphide bridge formation played a key role in RNA binding, offering an explanation why infectious virus cannot be rescued if cysteine residues are mutated, and that multiple sites may promote RNA binding.
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spelling pubmed-70928622020-03-25 Biophysical characterisation of the nucleocapsid protein from a highly pathogenic porcine reproductive and respiratory syndrome virus strain Jourdan, Stefanie S. Osorio, Fernando A. Hiscox, Julian A. Biochem Biophys Res Commun Article The arterivirus nucleocapsid (N) protein is a multifunctional protein that binds viral RNA for encapsidation and has potential roles in host cell processes. This study characterised the N protein from a highly virulent North American strain of porcine reproductive and respiratory syndrome virus (PRRSV). The association with viral RNA was mapped to defined motifs on the N protein. The results indicated that disulphide bridge formation played a key role in RNA binding, offering an explanation why infectious virus cannot be rescued if cysteine residues are mutated, and that multiple sites may promote RNA binding. Elsevier Inc. 2012-03-09 2012-01-28 /pmc/articles/PMC7092862/ /pubmed/22306009 http://dx.doi.org/10.1016/j.bbrc.2011.11.126 Text en Copyright © 2011 Elsevier Inc. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Jourdan, Stefanie S.
Osorio, Fernando A.
Hiscox, Julian A.
Biophysical characterisation of the nucleocapsid protein from a highly pathogenic porcine reproductive and respiratory syndrome virus strain
title Biophysical characterisation of the nucleocapsid protein from a highly pathogenic porcine reproductive and respiratory syndrome virus strain
title_full Biophysical characterisation of the nucleocapsid protein from a highly pathogenic porcine reproductive and respiratory syndrome virus strain
title_fullStr Biophysical characterisation of the nucleocapsid protein from a highly pathogenic porcine reproductive and respiratory syndrome virus strain
title_full_unstemmed Biophysical characterisation of the nucleocapsid protein from a highly pathogenic porcine reproductive and respiratory syndrome virus strain
title_short Biophysical characterisation of the nucleocapsid protein from a highly pathogenic porcine reproductive and respiratory syndrome virus strain
title_sort biophysical characterisation of the nucleocapsid protein from a highly pathogenic porcine reproductive and respiratory syndrome virus strain
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7092862/
https://www.ncbi.nlm.nih.gov/pubmed/22306009
http://dx.doi.org/10.1016/j.bbrc.2011.11.126
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