{ "abstract": "Giant viruses are large DNA viruses that infect unicellular and multicellular eukaryotes and form exceptionally large extracellular particles. (Meta)genomics and (meta)transcriptomics have provided insight into their diverse coding repertoire, but many of the proteins remain to be characterized as they lack homology with known proteins. Here, we integrate cross-linking mass spectrometry, quantitative proteomics, computational tools and cryo-EM data to characterize the protein architecture of intact melbournevirus particles. Based on this, we allocate 88 viral proteins to different virion sub-compartments and propose topologies of 25 inner membrane proteins. We assign eight components of the capsid in cryo-EM data, including proteins that tether the capsid shell to the membrane, reflecting key points in virion maturation. The data provide a valuable resource and demonstrate the power of an integrative approach to gain system-level structural insights into a poorly characterized biological system.", "abstract_shown": true, "affiliations": [ "Charité Universitätsmedizin Berlin, Berlin, Germany", "Department of Structural Biology, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany", "Charité Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany", "Research Group \"Structural Interactomics\", Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert-Roessle-Str. 0 325 Berlin, Germany", "In situ Structural Biology, Max Delbrück Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany", "Institute of Chemistry and Biochemistry, Freie Universität Berlin, Berlin, Germany", "Institute of Medical Physics and Biophysics, Charité Universitätsmedizin Berlin, Berlin, Germany", "In situ Structural Biology, Max Delbrück Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin 1125, Germany", "Institute of Chemistry and Biochemistry, Freie Universität Berlin, Takustraße 6, 1195 Berlin, Germany", "Department of Physiological Sciences, The Graduate University for Advanced Studies (SOKENDAI), Okazaki, Japan", "Exploratory Research Center on Life and Living System (ExCELLS), National Institutes of Natural Sciences (NINS), Okazaki, Japan", "National Institute for Physiological Sciences (NIPS), National Institute of Natural Sciences (NINS), Okazaki, Japan", "Department of Physiological Sciences, The Graduate University for Advanced Studies (SOKENDAI), 38 Nishigonaka, Myodaiji, Okazaki, Aichi 444-8585, Japan", "Exploratory Research Center on Life and Living System (ExCELLS), National Institutes of Natural Sciences (NINS), 38 Nishigonaka, Myodaiji, Okazaki, Aichi 444-8585, Japan", "National Institute for Physiological Sciences (NIPS), National Institute of Natural Sciences (NINS), 38 Nishigonaka, Myodaiji, Okazaki, Aichi 444-88, Japan", "Laboratory of Molecular Biophysics, Department of Cell and Molecular Biology, Uppsala University, Uppsala, Sweden", "Laboratory of Molecular Biophysics, Department of Cell and Molecular Biology, Uppsala University, Husargatan 3, SE-75124, Uppsala, Sweden", "Department of Structural Biology, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany. boris.bogdanow@charite.de", "Institute of Virology, Charité Universitätsmedizin Berlin, Freie Universität Berlin and Humboldt-Universität zu Berlin, Berlin, Germany. boris.bogdanow@charite.de", "Institute of Virology, Charité Universitätsmedizin Berlin, Freie Universität Berlin and Humboldt-Universität zu Berlin, Berlin, Germany", "Charité Universitätsmedizin Berlin, Berlin, Germany. fliu@fmp-berlin.de", "Department of Structural Biology, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany. fliu@fmp-berlin.de" ], "article_type": null, "arxiv": null, "author_total": 9, "authors": [ { "affs": [ 0, 1, 2, 3 ], "name": "Lars Mühlberg", "orcid": "0009-0008-8046-007X" }, { "affs": [ 1, 3 ], "name": "Julia Ruta", "orcid": "0009-0007-0524-6885" }, { "affs": [ 4, 5, 6, 7, 8 ], "name": "Vasilii Mikirtumov", "orcid": "0009-0004-6849-4825" }, { "affs": [ 9, 10, 11, 12, 13, 14 ], "name": "Raymond N. Burton‐Smith", "orcid": "0000-0002-1535-6419" }, { "affs": [ 9, 10, 11, 12, 13, 14 ], "name": "Kazuyoshi Murata", "orcid": "0000-0001-9446-3652" }, { "affs": [ 4, 6, 7 ], "name": "Mikhail Kudryashev", "orcid": "0000-0003-3550-6274" }, { "affs": [ 15, 16 ], "name": "Kenta Okamoto", "orcid": "0000-0002-4858-1196" }, { "affs": [ 17, 18, 19, 3 ], "name": "Boris Bogdanow", "orcid": "0000-0002-9634-7353" }, { "affs": [ 20, 21, 2, 3 ], "name": "Fan Liu", "orcid": "0000-0002-2358-549X" } ], "bibtex": "https://research.draconitic.com/paper/7stbd6c6k2pf4.bib", "cited_by": 5, "doi": "10.1038/s41467-026-74973-2", "fulltext_url": null, "id": "7stbd6c6k2pf4", "issns": [ "2041-1723" ], "landing_url": "https://doi.org/10.1038/s41467-026-74973-2", "language": "en", "licence": "CC-BY", "licence_label": "CC BY", "licence_source": "journal", "licence_url": "https://creativecommons.org/licenses/by/4.0/", "metadata_licence": null, "native_subjects": [ [ "openalex", "1607|Advanced Proteomics Techniques and Applications" ] ], "openalex": "W4411461176", "pdf_url": "https://www.nature.com/articles/s41467-026-74973-2.pdf", "pmcid": "PMC13365592", "pmid": "42443172", "published": "2026-07-13", "publisher": "Nature Portfolio", "ris": "https://research.draconitic.com/paper/7stbd6c6k2pf4.ris", "sources": [ { "first_seen": "2026-10-30T13:26:44Z", "native_id": "W4411461176", "source": "openalex", "url": "https://doi.org/10.1038/s41467-026-74973-2" } ], "subjects": [ { "field": "chemistry", "origin": "openalex:1607|Advanced Proteomics Techniques and Applications", "subfield": "physical" } ], "title": "Integrative structural interactomics reveals protein organization and structure in a giant virus", "title_text": "Integrative structural interactomics reveals protein organization and structure in a giant virus", "type": "peer-reviewed", "updated_at": "2026-11-03T13:20:28Z", "url": "https://research.draconitic.com/paper/7stbd6c6k2pf4", "venue": "Nature Communications", "versions": [] }