ArticleNature communications2025
Structural host-virus interactome profiling of intact infected cells.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed.
- Mapping in-cell protein contact sites reveals hijacking of paraspeckles during influenza A virus infection.Nature microbiology · 2026Article
- Article
- Optimized In-Solution and Gas-Phase Chemistry Enables High-Efficiency Interactome Mapping by DSBSO-Based Cross-Linking Mass Spectrometry.Angewandte Chemie (International ed. in English) · 2026Article
- AlphaFold models of host-pathogen interactions elucidate the prevalence and structural modes of molecular mimicry.bioRxiv : the preprint server for biology · 2025Article
- Interaction of human cytomegalovirus pUL52 with major components of the viral DNA encapsidation network underlines its essential role in genome cleavage-packaging.Journal of virology · 2025Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Virus-host protein-protein interactions (PPIs) are fundamental to viral infections, yet high-resolution identification of their structural and molecular determinants within the native context of intact infected cells has remained an unsolved challenge. Here, we provide detailed insights into the structural interactome of herpes simplex virus 1-infected human cells by combining in-cell cross-linking mass spectrometry with the selective enrichment of newly synthesized viral proteins. In productively infected cells, we obtain 739 PPIs based on 6,194 cross-links found across intracellular compartments and at the intact host endomembrane system. These structural host-virus interactome profiling (SHVIP) data resolve PPIs to the protein domain level and augment AlphaFold-based structural modeling, facilitating detailed predictions of PPI sites within structured and intrinsically disordered regions. Importantly, SHVIP captures parts of the virus-host PPI space that are elusive to traditional interaction proteomics approaches. Validation by molecular genetics confirms that these new SHVIP identifications are genuine virus-host PPIs occurring in the complex environment of intact infected cells.
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Registered trials
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