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

Created on 14 Jul 2026

Authors

Lars Mühlberg, Julia Ruta, Vasilii Mikirtumov, Raymond Burton-Smith, Kazuyoshi Murata, Mikhail Kudryashev, Kenta Okamoto, Boris Bogdanow, Fan Liu

Published in

Nature communications. Volume 17. Issue 1. Jul 13, 2026. Epub Jul 13, 2026.

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.

PMID:
42443172
Bibliographic data and abstract were imported from PubMed on 14 Jul 2026.

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