Atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virus.

Hendra virus (HeV) is a recently emerged severe human pathogen that belongs to the Henipavirus genus within the Paramyxoviridae family. The HeV genome is encapsidated by the nucleoprotein (N) within a helical nucleocapsid. Recruitment of the viral polymerase onto the nucleocapsid template relies on...

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Autores principales:	Guillaume Communie, Johnny Habchi, Filip Yabukarski, David Blocquel, Robert Schneider, Nicolas Tarbouriech, Nicolas Papageorgiou, Rob W H Ruigrok, Marc Jamin, Malene Ringkjøbing Jensen, Sonia Longhi, Martin Blackledge
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/f545aa83c6b2468d878c9bf9a27c5149
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spelling	oai:doaj.org-article:f545aa83c6b2468d878c9bf9a27c51492021-11-18T06:07:36ZAtomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virus.1553-73661553-737410.1371/journal.ppat.1003631https://doaj.org/article/f545aa83c6b2468d878c9bf9a27c51492013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24086133/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Hendra virus (HeV) is a recently emerged severe human pathogen that belongs to the Henipavirus genus within the Paramyxoviridae family. The HeV genome is encapsidated by the nucleoprotein (N) within a helical nucleocapsid. Recruitment of the viral polymerase onto the nucleocapsid template relies on the interaction between the C-terminal domain, N(TAIL), of N and the C-terminal X domain, XD, of the polymerase co-factor phosphoprotein (P). Here, we provide an atomic resolution description of the intrinsically disordered N(TAIL) domain in its isolated state and in intact nucleocapsids using nuclear magnetic resonance (NMR) spectroscopy. Using electron microscopy, we show that HeV nucleocapsids form herringbone-like structures typical of paramyxoviruses. We also report the crystal structure of XD of P that consists of a three-helix bundle. We study the interaction between N(TAIL) and XD using NMR titration experiments and provide a detailed mapping of the reciprocal binding sites. We show that the interaction is accompanied by α-helical folding of the molecular recognition element of N(TAIL) upon binding to a hydrophobic patch on the surface of XD. Finally, using solution NMR, we investigate the interaction between intact nucleocapsids and XD. Our results indicate that monomeric XD binds to N(TAIL) without triggering an additional unwinding of the nucleocapsid template. The present results provide a structural description at the atomic level of the protein-protein interactions required for transcription and replication of HeV, and the first direct observation of the interaction between the X domain of P and intact nucleocapsids in Paramyxoviridae.Guillaume CommunieJohnny HabchiFilip YabukarskiDavid BlocquelRobert SchneiderNicolas TarbouriechNicolas PapageorgiouRob W H RuigrokMarc JaminMalene Ringkjøbing JensenSonia LonghiMartin BlackledgePublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 9, Iss 9, p e1003631 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Guillaume Communie Johnny Habchi Filip Yabukarski David Blocquel Robert Schneider Nicolas Tarbouriech Nicolas Papageorgiou Rob W H Ruigrok Marc Jamin Malene Ringkjøbing Jensen Sonia Longhi Martin Blackledge Atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virus.
description	Hendra virus (HeV) is a recently emerged severe human pathogen that belongs to the Henipavirus genus within the Paramyxoviridae family. The HeV genome is encapsidated by the nucleoprotein (N) within a helical nucleocapsid. Recruitment of the viral polymerase onto the nucleocapsid template relies on the interaction between the C-terminal domain, N(TAIL), of N and the C-terminal X domain, XD, of the polymerase co-factor phosphoprotein (P). Here, we provide an atomic resolution description of the intrinsically disordered N(TAIL) domain in its isolated state and in intact nucleocapsids using nuclear magnetic resonance (NMR) spectroscopy. Using electron microscopy, we show that HeV nucleocapsids form herringbone-like structures typical of paramyxoviruses. We also report the crystal structure of XD of P that consists of a three-helix bundle. We study the interaction between N(TAIL) and XD using NMR titration experiments and provide a detailed mapping of the reciprocal binding sites. We show that the interaction is accompanied by α-helical folding of the molecular recognition element of N(TAIL) upon binding to a hydrophobic patch on the surface of XD. Finally, using solution NMR, we investigate the interaction between intact nucleocapsids and XD. Our results indicate that monomeric XD binds to N(TAIL) without triggering an additional unwinding of the nucleocapsid template. The present results provide a structural description at the atomic level of the protein-protein interactions required for transcription and replication of HeV, and the first direct observation of the interaction between the X domain of P and intact nucleocapsids in Paramyxoviridae.
format	article
author	Guillaume Communie Johnny Habchi Filip Yabukarski David Blocquel Robert Schneider Nicolas Tarbouriech Nicolas Papageorgiou Rob W H Ruigrok Marc Jamin Malene Ringkjøbing Jensen Sonia Longhi Martin Blackledge
author_facet	Guillaume Communie Johnny Habchi Filip Yabukarski David Blocquel Robert Schneider Nicolas Tarbouriech Nicolas Papageorgiou Rob W H Ruigrok Marc Jamin Malene Ringkjøbing Jensen Sonia Longhi Martin Blackledge
author_sort	Guillaume Communie
title	Atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virus.
title_short	Atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virus.
title_full	Atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virus.
title_fullStr	Atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virus.
title_full_unstemmed	Atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virus.
title_sort	atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of hendra virus.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/f545aa83c6b2468d878c9bf9a27c5149
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Atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virus.

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