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dc.contributor.authorBrillault, Lou
dc.contributor.authorJutras, Philippe V
dc.contributor.authorDashti, Noor
dc.contributor.authorThuenemann, Eva C
dc.contributor.authorMorgan, Garry
dc.contributor.authorLomonossoff, George P
dc.contributor.authorLandsberg, Michael J
dc.contributor.authorSainsbury, Frank
dc.date.accessioned2021-06-25T06:12:31Z
dc.date.available2021-06-25T06:12:31Z
dc.date.issued2017
dc.identifier.issn1936-0851
dc.identifier.doi10.1021/acsnano.6b07747
dc.identifier.urihttp://hdl.handle.net/10072/405383
dc.description.abstractUnderstanding capsid assembly following recombinant expression of viral structural proteins is critical to the design and modification of virus-like nanoparticles for biomedical and nanotechnology applications. Here, we use plant-based transient expression of the Bluetongue virus (BTV) structural proteins, VP3 and VP7, to obtain high yields of empty and green fluorescent protein (GFP)-encapsidating core-like particles (CLPs) from leaves. Single-particle cryo-electron microscopy of both types of particles revealed considerable differences in CLP structure compared to the crystal structure of infection-derived CLPs; in contrast, the two recombinant CLPs have an identical external structure. Using this insight, we exploited the unencumbered pore at the 5-fold axis of symmetry and the absence of encapsidated RNA to label the interior of empty CLPs with a fluorescent bioconjugate. CLPs containing 120 GFP molecules and those containing approximately 150 dye molecules were both shown to bind human integrin via a naturally occurring Arg-Gly-Asp motif found on an exposed loop of the VP7 trimeric spike. Furthermore, fluorescently labeled CLPs were shown to interact with a cell line overexpressing the surface receptor. Thus, BTV CLPs present themselves as a useful tool in targeted cargo delivery. These results highlight the importance of detailed structural analysis of VNPs in validating their molecular organization and the value of such analyses in aiding their design and further modification.
dc.description.peerreviewedYes
dc.languageEnglish
dc.publisherAmerican Chemical Society
dc.relation.ispartofpagefrom3476
dc.relation.ispartofpageto3484
dc.relation.ispartofissue4
dc.relation.ispartofjournalACS Nano
dc.relation.ispartofvolume11
dc.subject.keywordsScience & Technology
dc.subject.keywordsPhysical Sciences
dc.subject.keywordsTechnology
dc.subject.keywordsChemistry, Multidisciplinary
dc.subject.keywordsChemistry, Physical
dc.titleEngineering recombinant virus-like nanoparticles from plants for cellular delivery
dc.typeJournal article
dc.type.descriptionC1 - Articles
dcterms.bibliographicCitationBrillault, L; Jutras, PV; Dashti, N; Thuenemann, EC; Morgan, G; Lomonossoff, GP; Landsberg, MJ; Sainsbury, F, Engineering recombinant virus-like nanoparticles from plants for cellular delivery, ACS Nano, 2017, 11 (4), pp. 3476-3484
dc.date.updated2021-06-25T06:08:25Z
gro.hasfulltextNo Full Text
gro.griffith.authorSainsbury, Frank


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