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

Authors :
Zinzula, Luca
Beck, Florian
Camasta, Marianna
Bohn, Stefan
Liu, Chuan
Morado, Dustin
Bracher, Andreas
Plitzko, Juergen M.
Baumeister, Wolfgang
Source :
Nature Communications; 11/27/2024, Vol. 15 Issue 1, p1-11, 11p
Publication Year :
2024

Abstract

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. Zinzula et al. reconstituted the helical ribonucleoprotein complex of Marburg virus in vitro, and determined its structure by cryo-electron microscopy in a single-layer conformation that recapitulates the assembly of authentic filovirus particles. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
20411723
Volume :
15
Issue :
1
Database :
Complementary Index
Journal :
Nature Communications
Publication Type :
Academic Journal
Accession number :
181235891
Full Text :
https://doi.org/10.1038/s41467-024-54431-7