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 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.
Authors
- Kenta Okamoto (ORCID: https://orcid.org/0000-0002-4858-1196)
- Takeshi Noda (ORCID: https://orcid.org/0000-0002-0658-4663)
- Olga Dolnik (ORCID: https://orcid.org/0000-0001-7739-4798)
- Ai Hirabayashi (ORCID: https://orcid.org/0000-0002-6209-5960)
- Yuki Takamatsu
- Takanobu Kurashige
- Hu Shangfan
- Catarina Oda Harumi
Institutions
- Uppsala University (SE)
- Philipps University of Marburg (DE)
- Kyoto University (JP)
- Science for Life Laboratory (SE)
- Institute of Molecular Biology and Biophysics (RU)
- Nagasaki University (JP)
Publication Details
- Journal
- mBio
- Published
- 2025-09-22
- DOI
- https://doi.org/10.1128/mbio.01557-25
- Primary Topic
- Viral Infections and Outbreaks Research
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Philipps-Universität Marburg
- Japan Agency for Medical Research and Development
- Ichiro Kanehara Foundation for the Promotion of Medical Sciences and Medical Care
- Kurozumi Medical Foundation
- Japan Society for the Promotion of Science
- Institute of Medical Science, University of Tokyo