Cryo-EM structure of single-layered nucleoprotein-RNA complex from Marburg virus.

Autor: Zinzula L; Max Planck Institute of Biochemistry, Research Group Molecular Structural Biology, Martinsried, Germany. zinzula@biochem.mpg.de.; iHuman Institute, ShanghaiTech University, Shanghai, China. zinzula@biochem.mpg.de., Beck F; Max Planck Institute of Biochemistry, Research Group Molecular Structural Biology, Martinsried, Germany.; Max Planck Institute of Biochemistry, Research Group CryoEM Technology, Martinsried, Germany., Camasta M; Max Planck Institute of Biochemistry, Research Group Molecular Structural Biology, Martinsried, Germany., Bohn S; Max Planck Institute of Biochemistry, Research Group Molecular Structural Biology, Martinsried, Germany.; Institute of Structural Biology, Helmholtz Center Munich, Oberschleissheim, Germany., Liu C; Max Planck Institute of Biochemistry, Research Group Molecular Structural Biology, Martinsried, Germany., Morado D; Max Planck Institute of Biochemistry, Department of Cell and Virus Structure, Martinsried, Germany.; Stockholm University, Department of Biochemistry and Biophysics, Science for Life Laboratory, Stockholm, Sweden., Bracher A; Max Planck Institute of Biochemistry, Department of Cellular Biochemistry, Martinsried, Germany., Plitzko JM; Max Planck Institute of Biochemistry, Research Group Molecular Structural Biology, Martinsried, Germany.; Max Planck Institute of Biochemistry, Research Group CryoEM Technology, Martinsried, Germany., Baumeister W; Max Planck Institute of Biochemistry, Research Group Molecular Structural Biology, Martinsried, Germany. baumeist@biochem.mpg.de.; iHuman Institute, ShanghaiTech University, Shanghai, China. baumeist@biochem.mpg.de.
Jazyk: angličtina
Zdroj: Nature communications [Nat Commun] 2024 Nov 27; Vol. 15 (1), pp. 10307. Date of Electronic Publication: 2024 Nov 27.
DOI: 10.1038/s41467-024-54431-7
Abstrakt: Marburg virus (MARV) causes lethal hemorrhagic fever in humans, posing a threat to global health. We determined by cryogenic electron microscopy (cryo-EM) the MARV helical ribonucleoprotein (RNP) complex structure in single-layered conformation, which differs from the previously reported structure of a double-layered helix. Our findings illuminate novel RNP interactions and expand knowledge on MARV genome packaging and nucleocapsid assembly, both processes representing attractive targets for the development of antiviral therapeutics against MARV disease.
Competing Interests: Competing interests: The authors declare that they have no competing interests.
(© 2024. The Author(s).)
Databáze: MEDLINE
Externí odkaz: