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Integrative structural interactomics reveals protein organization and structure in a giant virus

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Item Type:Article
Title:Integrative structural interactomics reveals protein organization and structure in a giant virus
Creators: Mühlberg, Lars ORCID logoORCID: https://orcid.org/0009-0008-8046-007X, Ruta, Julia ORCID logoORCID: https://orcid.org/0009-0007-0524-6885, Mikirtumov, Vasilii ORCID logoORCID: https://orcid.org/0009-0004-6849-4825, Burton-Smith, Raymond ORCID logoORCID: https://orcid.org/0000-0002-1535-6419, Murata, Kazuyoshi ORCID logoORCID: https://orcid.org/0000-0001-9446-3652, Kudryashev, Mikhail ORCID logoORCID: https://orcid.org/0000-0003-3550-6274, Okamoto, Kenta ORCID logoORCID: https://orcid.org/0000-0002-4858-1196, Bogdanow, Boris ORCID logoORCID: https://orcid.org/0000-0002-9634-7353 and Liu, Fan ORCID logoORCID: https://orcid.org/0000-0002-2358-549X
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.
Keywords:Capsid, Capsid Proteins, Cryoelectron Microscopy, Giant Viruses, Mass Spectrometry, Proteomics, Viral Proteins, Virion
Source:Nature Communications
ISSN:2041-1723
Publisher:Nature Publishing Group
Volume:17
Number:1
Page Range:6139
Date:13 July 2026
Official Publication:https://doi.org/10.1038/s41467-026-74973-2
PubMed:View item in PubMed
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