ArticleJournal of virology2017
Crystal Structure of the Marburg Virus Nucleoprotein Core Domain Chaperoned by a VP35 Peptide Reveals a Conserved Drug Target for Filovirus.
Article in Journal of virology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 43 citations in OpenAlex.
- Discovery of three small-molecule inhibitors targetingThe Journal of general virology · 2025Article
- Molecular insights into nucleocapsid assembly and transport in Marburg and Ebola viruses.mBio · 2025Article
- Conserved Filovirus Proteins as Targets of Broad-Spectrum Antivirals.bioRxiv : the preprint server for biology · 2025Article
- Therapeutic advances in Marburg virus disease: from experimental treatments to vaccine development.Annals of medicine and surgery (2012) · 2025Review
- Cryo-EM structure of single-layered nucleoprotein-RNA complex from Marburg virus.Nature communications · 2024Article
- Cryoelectron microscopic structure of the nucleoprotein-RNA complex of the European filovirus, Lloviu virus.PNAS nexus · 2023Article
- Structural and biophysical characterization of the Borna disease virus 1 phosphoprotein.Acta crystallographica. Section F, Structural biology communications · 2023Article
- Ebola and Marburg virus VP35 coiled-coil validated as antiviral target by tripartite split-GFP complementation.iScience · 2022Article
- Article
- Assembly and transport of filovirus nucleocapsids.PLoS pathogens · 2022Review
- Structural insight into Marburg virus nucleoprotein-RNA complex formation.Nature communications · 2022Article
- The Nucleocapsid of Paramyxoviruses: Structure and Function of an Encapsidated Template.Viruses · 2021Review
- Review
- Distinct Genome Replication and Transcription Strategies within the Growing Filovirus Family.Journal of molecular biology · 2019Review
- Inhibition of Marburg Virus RNA Synthesis by a Synthetic Anti-VP35 Antibody.ACS infectious diseases · 2019Article
- Sudan Ebolavirus VP35-NP Crystal Structure Reveals a Potential Target for Pan-Filovirus Treatment.mBio · 2019Article
- Biochemical characterization of the respiratory syncytial virus NThe Journal of biological chemistry · 2019Article
- Virus and host interactions critical for filoviral RNA synthesis as therapeutic targets.Antiviral research · 2019Review
- Recent advances in marburgvirus research.F1000Research · 2019Review
- The Nucleoprotein and Phosphoprotein of Measles Virus.Frontiers in microbiology · 2019Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Filovirus nucleoprotein (NP), viral protein 35 (VP35), and polymerase L are essential for viral replication and nucleocapsid formation. Here, we identify a 28-residue peptide (NP binding peptide [NPBP]) from Marburg virus (MARV) VP35 through sequence alignment with previously identified Ebola virus (EBOV) NPBP, which bound to the core region (residues 18 to 344) of the N-terminal portion of MARV NP with high affinity. The crystal structure of the MARV NP core/NPBP complex at a resolution of 2.6 Å revealed that NPBP binds to the C-terminal region of the NP core via electrostatic and nonpolar interactions. Further structural analysis revealed that the MARV and EBOV NP cores hold a conserved binding pocket for NPBP, and this pocket could serve as a promising target for the design of universal drugs against filovirus infection. In addition, cross-binding assays confirmed that the NP core of MARV or EBOV can bind the NPBP from the other virus, although with moderately reduced binding affinities that result from termini that are distinct between the MARV and EBOV NPBPs.
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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.