Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/143163
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dc.contributor.authorHo, James Chin Shingen_US
dc.contributor.authorSteininger, Christophen_US
dc.contributor.authorHiew, Shu Huien_US
dc.contributor.authorKim, Min Chulen_US
dc.contributor.authorReimhult, Eriken_US
dc.contributor.authorMiserez, Alien_US
dc.contributor.authorCho, Nam-Joonen_US
dc.contributor.authorParikh, Atul N.en_US
dc.contributor.authorLiedberg, Boen_US
dc.date.accessioned2020-08-07T01:55:50Z-
dc.date.available2020-08-07T01:55:50Z-
dc.date.issued2019-
dc.identifier.citationHo, J. C. S., Steininger, C., Hiew, S. H., Kim, M. C., Reimhult, E., Miserez, A., ... Liedberg, B. (2019). Minimal reconstitution of membranous web induced by a vesicle–peptide sol–gel transition. Biomacromolecules, 20(4), 1709-1718. doi:10.1021/acs.biomac.9b00081en_US
dc.identifier.issn1525-7797en_US
dc.identifier.urihttps://hdl.handle.net/10356/143163-
dc.description.abstractPositive strand RNA viruses replicate in specialized niches called membranous web within the cytoplasm of host cells. These virus replication organelles sequester viral proteins, RNA, and a variety of host factors within a fluid, amorphous matrix of clusters of endoplasmic reticulum (ER) derived vesicles. They are thought to form by the actions of a nonstructural viral protein NS4B, which remodels the ER and produces dense lipid-protein condensates. Here, we used in vitro reconstitution to identify the minimal components and elucidate physical mechanisms driving the web formation. We found that the N-terminal amphipathic domain of NS4B (peptide 4BAH2) and phospholipid vesicles (∼100-200 nm in diameter) were sufficient to produce a gel-like, viscoelastic condensate. This condensate coexists with the surrounding aqueous phase and affords rapid exchange of molecules. Together, it recapitulates the essential properties of the virus-induced membranous web. Our data support a novel phase separation mechanism in which phospholipid vesicles provide a supramolecular template spatially organizing multiple self-associating peptides thereby generating programmable multivalency de novo and inducing macroscopic phase separation.en_US
dc.language.isoenen_US
dc.relation.ispartofBiomacromoleculesen_US
dc.rightsThis document is the Accepted Manuscript version of a Published Work that appeared in final form in Biomacromolecules, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acs.biomac.9b00081en_US
dc.subjectEngineering::Chemical engineeringen_US
dc.titleMinimal reconstitution of membranous web induced by a vesicle–peptide sol–gel transitionen_US
dc.typeJournal Articleen
dc.contributor.schoolSchool of Chemical and Biomedical Engineeringen_US
dc.contributor.schoolSchool of Materials Science and Engineeringen_US
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.contributor.organizationCentre for Biomimetic Sensor Scienceen_US
dc.identifier.doi10.1021/acs.biomac.9b00081-
dc.description.versionAccepted versionen_US
dc.identifier.pmid30856330-
dc.identifier.scopus2-s2.0-85064113333-
dc.identifier.issue4en_US
dc.identifier.volume20en_US
dc.identifier.spage1709en_US
dc.identifier.epage1718en_US
dc.subject.keywordsRNAen_US
dc.subject.keywordsVesicle-peptide Sol-gel Transitionen_US
item.fulltextWith Fulltext-
item.grantfulltextopen-
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