Molecular insights into nucleocapsid assembly and transport in Marburg and Ebola viruses

This study provides crucial insights into the molecular mechanisms of nucleocapsid assembly and transport in filoviruses, specifically Marburg virus (MARV) and Ebola virus (EBOV). Using advanced live-cell imaging, we uncovered how the conserved PPxPxY motif in nucleoprotein (NP) mediates its interac...

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Vydáno v:mBio Ročník 16; číslo 11; s. e0155725
Hlavní autoři: Takamatsu, Yuki, Dolnik, Olga, Hirabayashi, Ai, Okamoto, Kenta, Kurashige, Tomomi, Shangfan, Hu, Oda Harumi, Catarina, Noda, Takeshi
Médium: Journal Article
Jazyk:angličtina
Vydáno: United States American Society for Microbiology 12.11.2025
Témata:
Animals
Assembly and Maturation
Assembly Sites and Cellular Compartments
C-Terminus
Cell Biology
Cell Line
Cell migration
Ebola virus
Ebolavirus
Ebolavirus - genetics
Ebolavirus - physiology
Editor’s Pick
Epidemics
Filoviridae
Genomes
Humans
live-cell imaging
Marburg virus
Marburgvirus - genetics
Marburgvirus - physiology
Measles
Microscopy
Molecular modelling
NCLS
Nucleocapsid
Nucleocapsid - genetics
Nucleocapsid - metabolism
Nucleocapsid Proteins - genetics
Nucleocapsid Proteins - metabolism
Nucleocapsids
Nucleoproteins - genetics
Nucleoproteins - metabolism
Plasmids
Protein Binding
protein structure-function
Proteins
Replication
Research Article
RNA polymerase
Structural Proteins
Transcription Factors
Velocity
Viral Assembly in Host Cells
Viral Capsid Assembly
Viral Nucleoproteins
Viral Proteins
Viral Proteins - genetics
Viral Proteins - metabolism
Viral Structure
Virology
Virus Assembly
Virus Replication
Viruses
VP24 protein
Africa
Ebola virus
NCLS
protein structure-function
Marburg virus
live-cell imaging
ISSN:2150-7511, 2161-2129, 2150-7511
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Popis
Shrnutí:This study provides crucial insights into the molecular mechanisms of nucleocapsid assembly and transport in filoviruses, specifically Marburg virus (MARV) and Ebola virus (EBOV). Using advanced live-cell imaging, we uncovered how the conserved PPxPxY motif in nucleoprotein (NP) mediates its interactions with VP30, thereby regulating nucleocapsid formation and viral replication. Notably, while VP30’s role differs between MARV and EBOV, the underlying mechanism of NP-VP30 interaction via this motif appears conserved across filoviruses, making it a promising target for broad-spectrum antiviral strategies. These findings deepen our understanding of nucleocapsid protein compatibility and virus-host interactions, offering new avenues for therapeutic intervention against these deadly pathogens.
Bibliografie:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:2150-7511
2161-2129
2150-7511
DOI:10.1128/mbio.01557-25