RETICULON-LIKE PROTEIN B2 is a proviral factor co-opted for the biogenesis of viral replication organelles in plants

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dc.contributor.authorZhang, Qianshenen
dc.contributor.authorWen, Zhiyanen
dc.contributor.authorZhang, Xinen
dc.contributor.authorShe, Jiajieen
dc.contributor.authorWang, Xiaolingen
dc.contributor.authorGao, Zongyuen
dc.contributor.authorWang, Ruiqien
dc.contributor.authorZhao, Xiaofeien
dc.contributor.authorSu, Zhenen
dc.contributor.authorLi, Zhenen
dc.contributor.authorLi, Daweien
dc.contributor.authorWang, Xiaofengen
dc.contributor.authorZhang, Yongliangen
dc.date.accessioned2023-06-28T12:55:31Zen
dc.date.available2023-06-28T12:55:31Zen
dc.date.issued2023-05en
dc.description.abstractEndomembrane remodeling to form a viral replication complex (VRC) is crucial for a virus to establish infection in a host. Although the composition and function of VRCs have been intensively studied, host factors involved in the assembly of VRCs for plant RNA viruses have not been fully explored. TurboID-based proximity labeling (PL) has emerged as a robust tool for probing molecular interactions in planta. However, few studies have employed the TurboID-based PL technique for investigating plant virus replication. Here, we used Beet black scorch virus (BBSV), an endoplasmic reticulum (ER)-replicating virus, as a model and systematically investigated the composition of BBSV VRCs in Nicotiana benthamiana by fusing the TurboID enzyme to viral replication protein p23. Among the 185 identified p23-proximal proteins, the reticulon family of proteins showed high reproducibility in the mass spectrometry data sets. We focused on RETICULON-LIKE PROTEIN B2 (RTNLB2) and demonstrated its proviral functions in BBSV replication. We showed that RTNLB2 binds to p23, induces ER membrane curvature, and constricts ER tubules to facilitate the assembly of BBSV VRCs. Our comprehensive proximal interactome analysis of BBSV VRCs provides a resource for understanding plant viral replication and offers additional insights into the formation of membrane scaffolds for viral RNA synthesis. TurboID-based proximity labeling reveals the viral replication complex structure of a plant virus, unveiling a proviral function of RETICULON-LIKE PROTEIN B2 in viral replication complex formation.en
dc.description.versionPublished versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.doihttps://doi.org/10.1093/plcell/koad146en
dc.identifier.eissn1532-298Xen
dc.identifier.issn1040-4651en
dc.identifier.pmid37216674en
dc.identifier.urihttp://hdl.handle.net/10919/115556en
dc.language.isoenen
dc.publisherOxford University Pressen
dc.rightsCreative Commons Attribution-NonCommercial-NoDerivatives 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/en
dc.subjectmosaic-virusen
dc.subjectendoplasmic-reticulumen
dc.subjectamphipathic helixen
dc.subjecthosten
dc.subjectvisualizationen
dc.subjectconstructionen
dc.subjectmembranesen
dc.subjectrevealsen
dc.subjectclonesen
dc.subjectcellsen
dc.titleRETICULON-LIKE PROTEIN B2 is a proviral factor co-opted for the biogenesis of viral replication organelles in plantsen
dc.title.serialPlant Cellen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten

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