ArticleJournal of the American Chemical Society2023
RNA to Rule Them All: Critical Steps in Lassa Virus Ribonucleoparticle Assembly and Recruitment.
Article in Journal of the American Chemical Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Lassa Virus-A Persistent and Evolving Threat.Microorganisms · 2026Review
- Characterization of conserved residues in the mammarenavirus matrix protein Z using novel Lassa virus life cycle modelling assays.Scientific reports · 2026Article
- The kinetics of nsp7-11 polyprotein processing and impact on complexation with nsp16 among human coronaviruses.Nature communications · 2025Article
- Licoisoflavone B and glabridin from Glycyrrhiza glabra as potent nucleoprotein antagonists of Lassa virus: insights from molecular docking, dynamics simulation, PCA, and DFT studies.Journal, genetic engineering & biotechnology · 2025Article
- X-ray spectroscopy meets native mass spectrometry: probing gas-phase protein complexes.Physical chemistry chemical physics : PCCP · 2025Review
- Lassa virus protein-protein interactions as mediators of Lassa fever pathogenesis.Virology journal · 2025Review
- Overview of the 2023 Physical Virology Gordon Research Conference-Viruses at Multiple Levels of Complexity.Viruses · 2024Article
- Fusogenic structural changes in arenavirus glycoproteins are associated with viroporin activity.PLoS pathogens · 2023Article
Corrections and comments
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Authors and funding
7 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lassa virus is a negative-strand RNA virus with only four structural proteins that causes periodic outbreaks in West Africa. The nucleoprotein (NP) encapsidates the viral genome, forming ribonucleoprotein complexes (RNPs) together with the viral RNA and the L protein. RNPs must be continuously restructured during viral genome replication and transcription. The Z protein is important for membrane recruitment of RNPs, viral particle assembly, and budding and has also been shown to interact with the L protein. However, the interaction of NP, viral RNA, and Z is poorly understood. Here, we characterize the interactions between Lassa virus NP, Z, and RNA using structural mass spectrometry. We identify the presence of RNA as the driver for the disassembly of ring-like NP trimers, a storage form, into monomers to subsequently form higher order RNA-bound NP assemblies. We locate the interaction site of Z and NP and demonstrate that while NP binds Z independently of the presence of RNA, this interaction is pH-dependent. These data improve our understanding of RNP assembly, recruitment, and release in Lassa virus.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.