{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhang HJ"],"funding":["National Key R&D Program of China","the Key Program of the National Natural Science Foundation of China","National Natural Science Foundation of China"],"pagination":["e1007208"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6082576"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(7)"],"pubmed_abstract":["Epstein-Barr virus (EBV) is a human cancer-related virus closely associated with lymphoid and epithelial malignancies, and EBV glycoprotein B (gB) plays an essential role in viral entry into both B cells and epithelial cells by promoting cell-cell fusion. EBV gB is exclusively modified with high-mannose-linked N-glycans and primarily localizes to the endoplasmic reticulum (ER) with low levels on the plasma membrane (PM). However, the mechanism through which gB is regulated within host cells is largely unknown. Here, we report the identification of F-box only protein 2 (FBXO2), an SCF ubiquitin ligase substrate adaptor that preferentially binds high-mannose glycans and attenuates EBV infectivity by targeting N-glycosylated gB for degradation. gB possesses seven N-glycosylation sites, and FB"],"journal":["PLoS pathogens"],"pubmed_title":["Epstein-Barr virus activates F-box protein FBXO2 to limit viral infectivity by targeting glycoprotein B for degradation."],"pmcid":["PMC6082576"],"funding_grant_id":["No. 81430059","2017YFA0505600","2016YFC0902000","No. 81672980"],"pubmed_authors":["Tian J","Feng QS","Zhang HJ","Zhao B","Chen MY","Zeng MS","Xiang T","Zhang H","He GP","Feng L","Zhang X","Zeng YX","Qi XK","Yu X"],"additional_accession":[]},"is_claimable":false,"name":"Epstein-Barr virus activates F-box protein FBXO2 to limit viral infectivity by targeting glycoprotein B for degradation.","description":"Epstein-Barr virus (EBV) is a human cancer-related virus closely associated with lymphoid and epithelial malignancies, and EBV glycoprotein B (gB) plays an essential role in viral entry into both B cells and epithelial cells by promoting cell-cell fusion. EBV gB is exclusively modified with high-mannose-linked N-glycans and primarily localizes to the endoplasmic reticulum (ER) with low levels on the plasma membrane (PM). However, the mechanism through which gB is regulated within host cells is largely unknown. Here, we report the identification of F-box only protein 2 (FBXO2), an SCF ubiquitin ligase substrate adaptor that preferentially binds high-mannose glycans and attenuates EBV infectivity by targeting N-glycosylated gB for degradation. gB possesses seven N-glycosylation sites, and FB","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Jul","modification":"2026-04-07T14:50:26.654Z","creation":"2019-03-26T23:52:47Z"},"accession":"S-EPMC6082576","cross_references":{"pubmed":["30052682"],"doi":["10.1371/journal.ppat.1007208"]}}