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

• Published in: Nature communications 2024-11, Vol.15 (1), p.10307-11, Article 10307
• Main Authors: Zinzula, Luca, Beck, Florian, Camasta, Marianna, Bohn, Stefan, Liu, Chuan, Morado, Dustin, Bracher, Andreas, Plitzko, Juergen M., Baumeister, Wolfgang
• Format: Article
• Language: English
• Subjects: 101/28; 631/326/596; 631/535/1258/1259; 82/16; 82/29; 82/80; 82/83; Assembly; Biochemistry; Conformation; Cryoelectron Microscopy; Drug development; Electron microscopy; Genomes; Global health; Hemorrhagic fever; Humanities and Social Sciences; Humans; Infectious diseases; Knowledge representation; Marburgvirus - chemistry; Marburgvirus - metabolism; Marburgvirus - ultrastructure; Microscopy; Models, Molecular; multidisciplinary; Nucleocapsid - chemistry; Nucleocapsid - metabolism; Nucleocapsid - ultrastructure; Nucleocapsids; Nucleoproteins - chemistry; Nucleoproteins - metabolism; Nucleoproteins - ultrastructure; Packaging; Public health; Ribonucleoproteins - chemistry; Ribonucleoproteins - metabolism; Ribonucleoproteins - ultrastructure; RNA viruses; RNA, Viral - chemistry; RNA, Viral - genetics; RNA, Viral - metabolism; RNA, Viral - ultrastructure; Science; Science (multidisciplinary); Transmission electron microscopy; Viral diseases; Viral Proteins - chemistry; Viral Proteins - metabolism; Viral Proteins - ultrastructure; Virus Assembly; Viruses
• ISSN: 2041-1723; 2041-1723
• DOI: 10.1038/s41467-024-54431-7

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.