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TitleCryo-EM structure of single-layered nucleoprotein-RNA complex from Marburg virus.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 10307, Year 2024
Publish dateNov 27, 2024
AuthorsLuca Zinzula / Florian Beck / Marianna Camasta / Stefan Bohn / Chuan Liu / Dustin Morado / Andreas Bracher / Juergen M Plitzko / Wolfgang Baumeister /
PubMed AbstractMarburg 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) ...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.
External linksNat Commun / PubMed:39604358 / PubMed Central
MethodsEM (helical sym.) / EM (single particle)
Resolution3.1 - 3.2 Å
Structure data

50803

9fvd

EMDB-50803, PDB-9fvd:
Cryo-EM structure of single-layered nucleoprotein-RNA helical assembly from Marburg virus, trimeric repeat unit
Method: EM (helical sym.) / Resolution: 3.2 Å

EMDB-50804: Density for a protein trimer unit bound to RNA from a single-layered nucleoprotein-RNA helical assembly from Marburg virus
Method: EM (single particle) / Resolution: 3.1 Å

Source
  • Marburg virus - Musoke, Kenya, 1980
  • marburg virus - musoke
  • kenya, 1980
KeywordsVIRAL PROTEIN / RNA-binding protein

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