Membrane remodeling by the double-barrel scaffolding protein of poxvirus.

In contrast to most enveloped viruses, poxviruses produce infectious particles that do not acquire their internal lipid membrane by budding through cellular compartments. Instead, poxvirus immature particles are generated from atypical crescent-shaped precursors whose architecture and composition re...

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Autores principales:	Jae-Kyung Hyun, Cathy Accurso, Marcel Hijnen, Philipp Schult, Anne Pettikiriarachchi, Alok K Mitra, Fasséli Coulibaly
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/a6ba9e6d863e40cfaeaa097b72fe9f06
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spelling	oai:doaj.org-article:a6ba9e6d863e40cfaeaa097b72fe9f062021-11-04T05:51:28ZMembrane remodeling by the double-barrel scaffolding protein of poxvirus.1553-73661553-737410.1371/journal.ppat.1002239https://doaj.org/article/a6ba9e6d863e40cfaeaa097b72fe9f062011-09-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21931553/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374In contrast to most enveloped viruses, poxviruses produce infectious particles that do not acquire their internal lipid membrane by budding through cellular compartments. Instead, poxvirus immature particles are generated from atypical crescent-shaped precursors whose architecture and composition remain contentious. Here we describe the 2.6 Å crystal structure of vaccinia virus D13, a key structural component of the outer scaffold of viral crescents. D13 folds into two jellyrolls decorated by a head domain of novel fold. It assembles into trimers that are homologous to the double-barrel capsid proteins of adenovirus and lipid-containing icosahedral viruses. We show that, when tethered onto artificial membranes, D13 forms a honeycomb lattice and assembly products structurally similar to the viral crescents and immature particles. The architecture of the D13 honeycomb lattice and the lipid-remodeling abilities of D13 support a model of assembly that exhibits similarities with the giant mimivirus. Overall, these findings establish that the first committed step of poxvirus morphogenesis utilizes an ancestral lipid-remodeling strategy common to icosahedral DNA viruses infecting all kingdoms of life. Furthermore, D13 is the target of rifampicin and its structure will aid the development of poxvirus assembly inhibitors.Jae-Kyung HyunCathy AccursoMarcel HijnenPhilipp SchultAnne PettikiriarachchiAlok K MitraFasséli CoulibalyPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 7, Iss 9, p e1002239 (2011)
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 Jae-Kyung Hyun Cathy Accurso Marcel Hijnen Philipp Schult Anne Pettikiriarachchi Alok K Mitra Fasséli Coulibaly Membrane remodeling by the double-barrel scaffolding protein of poxvirus.
description	In contrast to most enveloped viruses, poxviruses produce infectious particles that do not acquire their internal lipid membrane by budding through cellular compartments. Instead, poxvirus immature particles are generated from atypical crescent-shaped precursors whose architecture and composition remain contentious. Here we describe the 2.6 Å crystal structure of vaccinia virus D13, a key structural component of the outer scaffold of viral crescents. D13 folds into two jellyrolls decorated by a head domain of novel fold. It assembles into trimers that are homologous to the double-barrel capsid proteins of adenovirus and lipid-containing icosahedral viruses. We show that, when tethered onto artificial membranes, D13 forms a honeycomb lattice and assembly products structurally similar to the viral crescents and immature particles. The architecture of the D13 honeycomb lattice and the lipid-remodeling abilities of D13 support a model of assembly that exhibits similarities with the giant mimivirus. Overall, these findings establish that the first committed step of poxvirus morphogenesis utilizes an ancestral lipid-remodeling strategy common to icosahedral DNA viruses infecting all kingdoms of life. Furthermore, D13 is the target of rifampicin and its structure will aid the development of poxvirus assembly inhibitors.
format	article
author	Jae-Kyung Hyun Cathy Accurso Marcel Hijnen Philipp Schult Anne Pettikiriarachchi Alok K Mitra Fasséli Coulibaly
author_facet	Jae-Kyung Hyun Cathy Accurso Marcel Hijnen Philipp Schult Anne Pettikiriarachchi Alok K Mitra Fasséli Coulibaly
author_sort	Jae-Kyung Hyun
title	Membrane remodeling by the double-barrel scaffolding protein of poxvirus.
title_short	Membrane remodeling by the double-barrel scaffolding protein of poxvirus.
title_full	Membrane remodeling by the double-barrel scaffolding protein of poxvirus.
title_fullStr	Membrane remodeling by the double-barrel scaffolding protein of poxvirus.
title_full_unstemmed	Membrane remodeling by the double-barrel scaffolding protein of poxvirus.
title_sort	membrane remodeling by the double-barrel scaffolding protein of poxvirus.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/a6ba9e6d863e40cfaeaa097b72fe9f06
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Membrane remodeling by the double-barrel scaffolding protein of poxvirus.

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