A study of "Super-resolution proximity labeling reveals antiviral protein network and its structural changes against SARS-CoV-2 viral proteins". Lee et al
SARS-CoV-2 replicates in human cells by interacting with host factors following infection. To understand the virus and host interactome, proximity, we introduce a super-resolution proximity labeling (SR-PL) method with “plug and playable” PL enzyme, TurboID-GBP (GFP binding protein) and we apply it...
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description | SARS-CoV-2 replicates in human cells by interacting with host factors following infection. To understand the virus and host interactome, proximity, we introduce a super-resolution proximity labeling (SR-PL) method with “plug and playable” PL enzyme, TurboID-GBP (GFP binding protein) and we apply it for interactome mapping of SARS-CoV-2 ORF3a and M, which generates highly perturbed ER structures. Through SR-PL analysis of the biotinylated interactome, 224 and 272 peptides are robustly identified as ORF3a and M interactomes, respectively. Within the ORF3a interactome, RNF5 co-localizes with ORF3a and generates ubiquitin modifications of ORF3a that can be involved in protein degradation. We also observe that the SARS-CoV-2 infection rate is efficiently reduced by the overexpression of RNF5 in host cells. The interactome data obtains using the SR-PL method are presented in https://sarscov2.spatiomics.org. We hope that our method will contribute to revealing virus–host interactions of other viruses in an efficient manner. |
doi_str_mv | 10.17632/wxy2fkp5w8.1 |
format | Dataset |
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The interactome data obtains using the SR-PL method are presented in https://sarscov2.spatiomics.org. We hope that our method will contribute to revealing virus–host interactions of other viruses in an efficient manner.</description><identifier>DOI: 10.17632/wxy2fkp5w8.1</identifier><language>eng</language><publisher>Mendeley</publisher><creationdate>2023</creationdate><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>780,1894</link.rule.ids><linktorsrc>$$Uhttps://commons.datacite.org/doi.org/10.17632/wxy2fkp5w8.1$$EView_record_in_DataCite.org$$FView_record_in_$$GDataCite.org$$Hfree_for_read</linktorsrc></links><search><creatorcontrib>Yun-Bin Lee</creatorcontrib><title>A study of "Super-resolution proximity labeling reveals antiviral protein network and its structural changes against SARS-CoV-2 viral proteins". Lee et al</title><description>SARS-CoV-2 replicates in human cells by interacting with host factors following infection. To understand the virus and host interactome, proximity, we introduce a super-resolution proximity labeling (SR-PL) method with “plug and playable” PL enzyme, TurboID-GBP (GFP binding protein) and we apply it for interactome mapping of SARS-CoV-2 ORF3a and M, which generates highly perturbed ER structures. Through SR-PL analysis of the biotinylated interactome, 224 and 272 peptides are robustly identified as ORF3a and M interactomes, respectively. Within the ORF3a interactome, RNF5 co-localizes with ORF3a and generates ubiquitin modifications of ORF3a that can be involved in protein degradation. We also observe that the SARS-CoV-2 infection rate is efficiently reduced by the overexpression of RNF5 in host cells. The interactome data obtains using the SR-PL method are presented in https://sarscov2.spatiomics.org. 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Lee et al</title><author>Yun-Bin Lee</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-datacite_primary_10_17632_wxy2fkp5w8_13</frbrgroupid><rsrctype>datasets</rsrctype><prefilter>datasets</prefilter><language>eng</language><creationdate>2023</creationdate><toplevel>online_resources</toplevel><creatorcontrib>Yun-Bin Lee</creatorcontrib><collection>DataCite (Open Access)</collection><collection>DataCite</collection></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Yun-Bin Lee</au><format>book</format><genre>unknown</genre><ristype>DATA</ristype><title>A study of "Super-resolution proximity labeling reveals antiviral protein network and its structural changes against SARS-CoV-2 viral proteins". Lee et al</title><date>2023-06-26</date><risdate>2023</risdate><abstract>SARS-CoV-2 replicates in human cells by interacting with host factors following infection. To understand the virus and host interactome, proximity, we introduce a super-resolution proximity labeling (SR-PL) method with “plug and playable” PL enzyme, TurboID-GBP (GFP binding protein) and we apply it for interactome mapping of SARS-CoV-2 ORF3a and M, which generates highly perturbed ER structures. Through SR-PL analysis of the biotinylated interactome, 224 and 272 peptides are robustly identified as ORF3a and M interactomes, respectively. Within the ORF3a interactome, RNF5 co-localizes with ORF3a and generates ubiquitin modifications of ORF3a that can be involved in protein degradation. We also observe that the SARS-CoV-2 infection rate is efficiently reduced by the overexpression of RNF5 in host cells. The interactome data obtains using the SR-PL method are presented in https://sarscov2.spatiomics.org. 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title | A study of "Super-resolution proximity labeling reveals antiviral protein network and its structural changes against SARS-CoV-2 viral proteins". Lee et al |
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