Intrinsically-disordered N-termini in human parechovirus 1 capsid proteins bind encapsidated RNA

Abstract Human parechoviruses (HPeV) are picornaviruses with a highly-ordered RNA genome contained within icosahedrally-symmetric capsids. Ordered RNA structures have recently been shown to interact with capsid proteins VP1 and VP3 and facilitate virus assembly in HPeV1. Using an assay that combines...

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Autores principales:	Shabih Shakeel, James D. Evans, Mark Hazelbaker, C. Cheng Kao, Robert C. Vaughan, Sarah J. Butcher
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/c61882b4e82648e0b67f4e7c833cfd5e
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spelling	oai:doaj.org-article:c61882b4e82648e0b67f4e7c833cfd5e2021-12-02T11:40:53ZIntrinsically-disordered N-termini in human parechovirus 1 capsid proteins bind encapsidated RNA10.1038/s41598-018-23552-72045-2322https://doaj.org/article/c61882b4e82648e0b67f4e7c833cfd5e2018-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-23552-7https://doaj.org/toc/2045-2322Abstract Human parechoviruses (HPeV) are picornaviruses with a highly-ordered RNA genome contained within icosahedrally-symmetric capsids. Ordered RNA structures have recently been shown to interact with capsid proteins VP1 and VP3 and facilitate virus assembly in HPeV1. Using an assay that combines reversible cross-linking, RNA affinity purification and peptide mass fingerprinting (RCAP), we mapped the RNA-interacting regions of the capsid proteins from the whole HPeV1 virion in solution. The intrinsically-disordered N-termini of capsid proteins VP1 and VP3, and unexpectedly, VP0, were identified to interact with RNA. Comparing these results to those obtained using recombinantly-expressed VP0 and VP1 confirmed the virion binding regions, and revealed unique RNA binding regions in the isolated VP0 not previously observed in the crystal structure of HPeV1. We used RNA fluorescence anisotropy to confirm the RNA-binding competency of each of the capsid proteins’ N-termini. These findings suggests that dynamic interactions between the viral RNA and the capsid proteins modulate virus assembly, and suggest a novel role for VP0.Shabih ShakeelJames D. EvansMark HazelbakerC. Cheng KaoRobert C. VaughanSarah J. ButcherNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-10 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Shabih Shakeel James D. Evans Mark Hazelbaker C. Cheng Kao Robert C. Vaughan Sarah J. Butcher Intrinsically-disordered N-termini in human parechovirus 1 capsid proteins bind encapsidated RNA
description	Abstract Human parechoviruses (HPeV) are picornaviruses with a highly-ordered RNA genome contained within icosahedrally-symmetric capsids. Ordered RNA structures have recently been shown to interact with capsid proteins VP1 and VP3 and facilitate virus assembly in HPeV1. Using an assay that combines reversible cross-linking, RNA affinity purification and peptide mass fingerprinting (RCAP), we mapped the RNA-interacting regions of the capsid proteins from the whole HPeV1 virion in solution. The intrinsically-disordered N-termini of capsid proteins VP1 and VP3, and unexpectedly, VP0, were identified to interact with RNA. Comparing these results to those obtained using recombinantly-expressed VP0 and VP1 confirmed the virion binding regions, and revealed unique RNA binding regions in the isolated VP0 not previously observed in the crystal structure of HPeV1. We used RNA fluorescence anisotropy to confirm the RNA-binding competency of each of the capsid proteins’ N-termini. These findings suggests that dynamic interactions between the viral RNA and the capsid proteins modulate virus assembly, and suggest a novel role for VP0.
format	article
author	Shabih Shakeel James D. Evans Mark Hazelbaker C. Cheng Kao Robert C. Vaughan Sarah J. Butcher
author_facet	Shabih Shakeel James D. Evans Mark Hazelbaker C. Cheng Kao Robert C. Vaughan Sarah J. Butcher
author_sort	Shabih Shakeel
title	Intrinsically-disordered N-termini in human parechovirus 1 capsid proteins bind encapsidated RNA
title_short	Intrinsically-disordered N-termini in human parechovirus 1 capsid proteins bind encapsidated RNA
title_full	Intrinsically-disordered N-termini in human parechovirus 1 capsid proteins bind encapsidated RNA
title_fullStr	Intrinsically-disordered N-termini in human parechovirus 1 capsid proteins bind encapsidated RNA
title_full_unstemmed	Intrinsically-disordered N-termini in human parechovirus 1 capsid proteins bind encapsidated RNA
title_sort	intrinsically-disordered n-termini in human parechovirus 1 capsid proteins bind encapsidated rna
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/c61882b4e82648e0b67f4e7c833cfd5e
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Intrinsically-disordered N-termini in human parechovirus 1 capsid proteins bind encapsidated RNA

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