Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A

Avian influenza polymerase undergoes host adaptation in order to efficiently replicate in human cells. Here, the authors use NMR spectroscopy and quantitative ensemble modelling to describe the highly dynamic assemblies formed by the human-adapted or avian-adapted C-terminal domains with the respect...

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Autores principales:	Aldo R. Camacho-Zarco, Sissy Kalayil, Damien Maurin, Nicola Salvi, Elise Delaforge, Sigrid Milles, Malene Ringkjøbing Jensen, Darren J. Hart, Stephen Cusack, Martin Blackledge
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/f3b9b8f89aab4c209ce56f87f7cfa567
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spelling	oai:doaj.org-article:f3b9b8f89aab4c209ce56f87f7cfa5672021-12-02T16:43:46ZMolecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A10.1038/s41467-020-17407-x2041-1723https://doaj.org/article/f3b9b8f89aab4c209ce56f87f7cfa5672020-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-17407-xhttps://doaj.org/toc/2041-1723Avian influenza polymerase undergoes host adaptation in order to efficiently replicate in human cells. Here, the authors use NMR spectroscopy and quantitative ensemble modelling to describe the highly dynamic assemblies formed by the human-adapted or avian-adapted C-terminal domains with the respective ANP32A host proteins.Aldo R. Camacho-ZarcoSissy KalayilDamien MaurinNicola SalviElise DelaforgeSigrid MillesMalene Ringkjøbing JensenDarren J. HartStephen CusackMartin BlackledgeNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Aldo R. Camacho-Zarco Sissy Kalayil Damien Maurin Nicola Salvi Elise Delaforge Sigrid Milles Malene Ringkjøbing Jensen Darren J. Hart Stephen Cusack Martin Blackledge Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A
description	Avian influenza polymerase undergoes host adaptation in order to efficiently replicate in human cells. Here, the authors use NMR spectroscopy and quantitative ensemble modelling to describe the highly dynamic assemblies formed by the human-adapted or avian-adapted C-terminal domains with the respective ANP32A host proteins.
format	article
author	Aldo R. Camacho-Zarco Sissy Kalayil Damien Maurin Nicola Salvi Elise Delaforge Sigrid Milles Malene Ringkjøbing Jensen Darren J. Hart Stephen Cusack Martin Blackledge
author_facet	Aldo R. Camacho-Zarco Sissy Kalayil Damien Maurin Nicola Salvi Elise Delaforge Sigrid Milles Malene Ringkjøbing Jensen Darren J. Hart Stephen Cusack Martin Blackledge
author_sort	Aldo R. Camacho-Zarco
title	Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A
title_short	Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A
title_full	Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A
title_fullStr	Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A
title_full_unstemmed	Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A
title_sort	molecular basis of host-adaptation interactions between influenza virus polymerase pb2 subunit and anp32a
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/f3b9b8f89aab4c209ce56f87f7cfa567
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Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A

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