Identification of plasticity and interactions of a highly conserved motif within a picornavirus capsid precursor required for virus infectivity

Abstract The picornavirus family includes poliovirus (PV) (genus: enterovirus), human rhinoviruses (enterovirus) and foot-and-mouth disease virus (FMDV) (aphthovirus). These are responsible for important human and animal health concerns worldwide including poliomyelitis, the common cold and foot-and...

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Autores principales:	Thea Kristensen, Graham J. Belsham
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/161881490bc54ca9982af8bcb41a3b2d
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spelling	oai:doaj.org-article:161881490bc54ca9982af8bcb41a3b2d2021-12-02T15:09:38ZIdentification of plasticity and interactions of a highly conserved motif within a picornavirus capsid precursor required for virus infectivity10.1038/s41598-019-48170-92045-2322https://doaj.org/article/161881490bc54ca9982af8bcb41a3b2d2019-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-019-48170-9https://doaj.org/toc/2045-2322Abstract The picornavirus family includes poliovirus (PV) (genus: enterovirus), human rhinoviruses (enterovirus) and foot-and-mouth disease virus (FMDV) (aphthovirus). These are responsible for important human and animal health concerns worldwide including poliomyelitis, the common cold and foot-and-mouth disease (FMD) respectively. In picornavirus particles, the positive-sense RNA genome (ca. 7–9 kb) is packaged within a protein shell (capsid) usually consisting of three surface exposed proteins, VP1, VP2 and VP3 plus the internal VP4, which are generated following cleavage of the capsid precursor by a virus-encoded protease. We have previously identified a motif near the C-terminus of FMDV VP1 that is required for capsid precursor processing. This motif is highly conserved among other picornaviruses, and is also likely to be important for their capsid precursor processing. We have now determined the plasticity of residues within this motif for virus infectivity and found an important interaction between FMDV residue VP1 R188 within this conserved motif and residue W129 in VP2 that is adjacent in the virus capsid. The FMDV (VP1 R188A) mutant virus has only been rescued with the secondary substitution VP2 W129R. This additional change compensates for the defect resulting from the VP1 R188A substitution and restored both capsid precursor processing and virus viability.Thea KristensenGraham J. BelshamNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 9, Iss 1, Pp 1-10 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Thea Kristensen Graham J. Belsham Identification of plasticity and interactions of a highly conserved motif within a picornavirus capsid precursor required for virus infectivity
description	Abstract The picornavirus family includes poliovirus (PV) (genus: enterovirus), human rhinoviruses (enterovirus) and foot-and-mouth disease virus (FMDV) (aphthovirus). These are responsible for important human and animal health concerns worldwide including poliomyelitis, the common cold and foot-and-mouth disease (FMD) respectively. In picornavirus particles, the positive-sense RNA genome (ca. 7–9 kb) is packaged within a protein shell (capsid) usually consisting of three surface exposed proteins, VP1, VP2 and VP3 plus the internal VP4, which are generated following cleavage of the capsid precursor by a virus-encoded protease. We have previously identified a motif near the C-terminus of FMDV VP1 that is required for capsid precursor processing. This motif is highly conserved among other picornaviruses, and is also likely to be important for their capsid precursor processing. We have now determined the plasticity of residues within this motif for virus infectivity and found an important interaction between FMDV residue VP1 R188 within this conserved motif and residue W129 in VP2 that is adjacent in the virus capsid. The FMDV (VP1 R188A) mutant virus has only been rescued with the secondary substitution VP2 W129R. This additional change compensates for the defect resulting from the VP1 R188A substitution and restored both capsid precursor processing and virus viability.
format	article
author	Thea Kristensen Graham J. Belsham
author_facet	Thea Kristensen Graham J. Belsham
author_sort	Thea Kristensen
title	Identification of plasticity and interactions of a highly conserved motif within a picornavirus capsid precursor required for virus infectivity
title_short	Identification of plasticity and interactions of a highly conserved motif within a picornavirus capsid precursor required for virus infectivity
title_full	Identification of plasticity and interactions of a highly conserved motif within a picornavirus capsid precursor required for virus infectivity
title_fullStr	Identification of plasticity and interactions of a highly conserved motif within a picornavirus capsid precursor required for virus infectivity
title_full_unstemmed	Identification of plasticity and interactions of a highly conserved motif within a picornavirus capsid precursor required for virus infectivity
title_sort	identification of plasticity and interactions of a highly conserved motif within a picornavirus capsid precursor required for virus infectivity
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/161881490bc54ca9982af8bcb41a3b2d
work_keys_str_mv	AT theakristensen identificationofplasticityandinteractionsofahighlyconservedmotifwithinapicornaviruscapsidprecursorrequiredforvirusinfectivity AT grahamjbelsham identificationofplasticityandinteractionsofahighlyconservedmotifwithinapicornaviruscapsidprecursorrequiredforvirusinfectivity
_version_	1718387798386409472

Identification of plasticity and interactions of a highly conserved motif within a picornavirus capsid precursor required for virus infectivity

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