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dc.contributor.authorMullapudi, Edukondalu
dc.contributor.authorFüzik, Tibor
dc.contributor.authorPřidal, Antonín
dc.contributor.authorPlevka, Pavel
dc.date.accessioned2017-07-11T13:09:44Z
dc.date.available2017-07-11T13:09:44Z
dc.date.issued2017-02-15
dc.identifier.citationCryo-electron Microscopy Study of the Genome Release of the Dicistrovirus Israeli Acute Bee Paralysis Virus. 2017, 91 (4) J. Virol.en
dc.identifier.issn1098-5514
dc.identifier.pmid27928006
dc.identifier.doi10.1128/JVI.02060-16
dc.identifier.urihttp://hdl.handle.net/10033/621006
dc.description.abstractViruses of the family Dicistroviridae can cause substantial economic damage by infecting agriculturally important insects. Israeli acute bee paralysis virus (IAPV) causes honeybee colony collapse disorder in the United States. High-resolution molecular details of the genome delivery mechanism of dicistroviruses are unknown. Here we present a cryo-electron microscopy analysis of IAPV virions induced to release their genomes in vitro We determined structures of full IAPV virions primed to release their genomes to a resolution of 3.3 Å and of empty capsids to a resolution of 3.9 Å. We show that IAPV does not form expanded A particles before genome release as in the case of related enteroviruses of the family Picornaviridae The structural changes observed in the empty IAPV particles include detachment of the VP4 minor capsid proteins from the inner face of the capsid and partial loss of the structure of the N-terminal arms of the VP2 capsid proteins. Unlike the case for many picornaviruses, the empty particles of IAPV are not expanded relative to the native virions and do not contain pores in their capsids that might serve as channels for genome release. Therefore, rearrangement of a unique region of the capsid is probably required for IAPV genome release.
dc.language.isoenen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subject.meshAnimalsen
dc.subject.meshBeesen
dc.subject.meshCapsiden
dc.subject.meshCapsid Proteinsen
dc.subject.meshCryoelectron Microscopyen
dc.subject.meshDicistroviridaeen
dc.subject.meshGenome, Viralen
dc.subject.meshModels, Molecularen
dc.subject.meshProtein Conformationen
dc.subject.meshVirionen
dc.subject.meshVirus Assemblyen
dc.subject.meshVirus Uncoatingen
dc.titleCryo-electron Microscopy Study of the Genome Release of the Dicistrovirus Israeli Acute Bee Paralysis Virus.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany.en
dc.identifier.journalJournal of virologyen
refterms.dateFOA2017-07-31T00:00:00Z
html.description.abstractViruses of the family Dicistroviridae can cause substantial economic damage by infecting agriculturally important insects. Israeli acute bee paralysis virus (IAPV) causes honeybee colony collapse disorder in the United States. High-resolution molecular details of the genome delivery mechanism of dicistroviruses are unknown. Here we present a cryo-electron microscopy analysis of IAPV virions induced to release their genomes in vitro We determined structures of full IAPV virions primed to release their genomes to a resolution of 3.3 Å and of empty capsids to a resolution of 3.9 Å. We show that IAPV does not form expanded A particles before genome release as in the case of related enteroviruses of the family Picornaviridae The structural changes observed in the empty IAPV particles include detachment of the VP4 minor capsid proteins from the inner face of the capsid and partial loss of the structure of the N-terminal arms of the VP2 capsid proteins. Unlike the case for many picornaviruses, the empty particles of IAPV are not expanded relative to the native virions and do not contain pores in their capsids that might serve as channels for genome release. Therefore, rearrangement of a unique region of the capsid is probably required for IAPV genome release.


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