Differential phosphorylation and n-terminal configuration of capsid subunits in parvovirus assembly and viral trafficking
dc.contributor.author | Gil-Ranedo, J | |
dc.contributor.author | Hernando, E | |
dc.contributor.author | Valle, N | |
dc.contributor.author | Riolobos, L | |
dc.contributor.author | Maroto, B | |
dc.contributor.author | Almendral, JM | |
dc.date.accessioned | 2018-10-24T08:25:48Z | |
dc.date.available | 2018-10-24T08:25:48Z | |
dc.date.issued | 2018-05 | |
dc.identifier.issn | 0042-6822 | |
dc.identifier.issn | 1096-0341 | |
dc.identifier.other | C | |
dc.identifier.uri | http://hdl.handle.net/10026.1/12599 | |
dc.description | publisher: Elsevier articletitle: Differential phosphorylation and n-terminal configuration of capsid subunits in parvovirus assembly and viral trafficking journaltitle: Virology articlelink: http://dx.doi.org/10.1016/j.virol.2018.02.018 content_type: article copyright: © 2018 Elsevier Inc. All rights reserved. | |
dc.description.abstract |
The T1 parvovirus Minute Virus of Mice (MVM) was used to study the roles that phosphorylation and N-terminal domains (Nt) configuration of capsid subunits may play in icosahedral nuclear viruses assembly. In synchronous MVM infection, capsid subunits newly assembled as two types of cytoplasmic trimeric intermediates (3VP2, and 1VP1:2VP2) harbored a VP1 phosphorylation level fivefold higher than that of VP2, and hidden Nt. Upon nuclear translocation at S phase, VP1-Nt became exposed in the heterotrimer and subsequent subviral assembly intermediates. Empty capsid subunits showed a phosphorylation level restored to VP1:VP2 stoichiometry, and the Nt concealed in their interior. However ssDNA-filled virus maturing at S/G2 lacked VP1 phosphorylation and one major VP2 phosphopeptide, and exposed VP2-Nt. Endosomal VP2-Nt cleavage resulted in VP3 subunits devoid of any phospholabel, implying that incoming viral particles specifically harbor a low phosphorylation status. Phosphorylation provides a mechanistic coupling of parvovirus nuclear assembly to the cell cycle. | |
dc.format.extent | 184-194 | |
dc.format.medium | Print-Electronic | |
dc.language | en | |
dc.language.iso | en | |
dc.publisher | Elsevier | |
dc.subject | Parvovirus | |
dc.subject | Capsid phosphorylation | |
dc.subject | Nt configuration | |
dc.subject | Assembly | |
dc.subject | Maturation | |
dc.subject | Viral trafficking | |
dc.title | Differential phosphorylation and n-terminal configuration of capsid subunits in parvovirus assembly and viral trafficking | |
dc.type | journal-article | |
dc.type | Journal Article | |
dc.type | Research Support, Non-U.S. Gov't | |
plymouth.author-url | https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000431388000020&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=11bb513d99f797142bcfeffcc58ea008 | |
plymouth.volume | 518 | |
plymouth.publication-status | Published | |
plymouth.journal | Virology | |
dc.identifier.doi | 10.1016/j.virol.2018.02.018 | |
plymouth.organisational-group | /Plymouth | |
plymouth.organisational-group | /Plymouth/Faculty of Health | |
plymouth.organisational-group | /Plymouth/Faculty of Health/Peninsula Medical School | |
plymouth.organisational-group | /Plymouth/REF 2021 Researchers by UoA | |
plymouth.organisational-group | /Plymouth/REF 2021 Researchers by UoA/UoA01 Clinical Medicine | |
plymouth.organisational-group | /Plymouth/Users by role | |
plymouth.organisational-group | /Plymouth/Users by role/Academics | |
dc.publisher.place | United States | |
dcterms.dateAccepted | 2018-02-21 | |
dc.rights.embargodate | 2019-3-15 | |
dc.identifier.eissn | 1096-0341 | |
dc.rights.embargoperiod | Not known | |
rioxxterms.versionofrecord | 10.1016/j.virol.2018.02.018 | |
rioxxterms.licenseref.uri | http://www.rioxx.net/licenses/all-rights-reserved | |
rioxxterms.licenseref.startdate | 2018-05 | |
rioxxterms.type | Journal Article/Review |