{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chihara A"],"funding":["National Institute for Physiological Sciences","Svenska Forskningsrådet Formas","Exploratory Research Center on Life and Living Systems, National Institutes of Natural Sciences","Royal Swedish Academy of Sciences","Swedish Foundation for International Cooperation in Research and Higher Education","Japan Society for the Promotion of Science"],"pagination":["21428"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9742146"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(1)"],"pubmed_abstract":["Marseilleviridae is a family of giant viruses, showing a characteristic internal membrane with extrusions underneath the icosahedral vertices. However, such large objects, with a maximum diameter of 250 nm are technically difficult to examine at sub-nanometre resolution by cryo-electron microscopy. Here, we tested the utility of 1 MV high-voltage cryo-EM (cryo-HVEM) for single particle structural analysis (SPA) of giant viruses using tokyovirus, a species of Marseilleviridae, and revealed the capsid structure at 7.7 Å resolution. The capsid enclosing the viral DNA consisted primarily of four layers: (1) major capsid proteins (MCPs) and penton proteins, (2) minor capsid proteins (mCPs), (3) scaffold protein components (ScPCs), and (4) internal membrane. The mCPs showed a novel capsid lattice consisting of eight protein components. ScPCs connecting the icosahedral vertices supported the formation of the membrane extrusions, and possibly act like tape measure proteins reported in other giant viruses. The density on top of the MCP trimer was suggested to include glycoproteins. This is the first attempt at cryo-HVEM SPA. We found the primary limitations to be the lack of automated data acquisition and software support for collection and processing and thus achievable resolution. However, the results pave the way for using cryo-HVEM for structural analysis of larger biological specimens."],"journal":["Scientific reports"],"pubmed_title":["A novel capsid protein network allows the characteristic internal membrane structure of Marseilleviridae giant viruses."],"pmcid":["PMC9742146"],"funding_grant_id":["JA2014-5721","20-239","2018-00421","JP19H04845","BS2018-0053","20-004"],"pubmed_authors":["Mitsuoka K","Okamoto K","Murata K","Chihara A","Kajimura N","Song C","Burton-Smith RN"],"additional_accession":[]},"is_claimable":false,"name":"A novel capsid protein network allows the characteristic internal membrane structure of Marseilleviridae giant viruses.","description":"Marseilleviridae is a family of giant viruses, showing a characteristic internal membrane with extrusions underneath the icosahedral vertices. However, such large objects, with a maximum diameter of 250 nm are technically difficult to examine at sub-nanometre resolution by cryo-electron microscopy. Here, we tested the utility of 1 MV high-voltage cryo-EM (cryo-HVEM) for single particle structural analysis (SPA) of giant viruses using tokyovirus, a species of Marseilleviridae, and revealed the capsid structure at 7.7 Å resolution. The capsid enclosing the viral DNA consisted primarily of four layers: (1) major capsid proteins (MCPs) and penton proteins, (2) minor capsid proteins (mCPs), (3) scaffold protein components (ScPCs), and (4) internal membrane. The mCPs showed a novel capsid lattice consisting of eight protein components. ScPCs connecting the icosahedral vertices supported the formation of the membrane extrusions, and possibly act like tape measure proteins reported in other giant viruses. The density on top of the MCP trimer was suggested to include glycoproteins. This is the first attempt at cryo-HVEM SPA. We found the primary limitations to be the lack of automated data acquisition and software support for collection and processing and thus achievable resolution. However, the results pave the way for using cryo-HVEM for structural analysis of larger biological specimens.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2026-05-29T18:52:18.397Z","creation":"2025-06-01T01:56:08.017Z"},"accession":"S-EPMC9742146","cross_references":{"pubmed":["36504202"],"doi":["10.1038/s41598-022-24651-2"]}}