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.
Marburg virus (MARV) is an enveloped, non-segmented, single-stranded negative-sense RNA (ssRNA -) virus that belongs to the Filoviridae family, order Mononegavirales, and causes lethal disease in humans and non-human primates1. Its discovery dates to 1967, when in Marburg and Frankfurt (Germany), and in Belgrade (Yugoslavia, now Serbia), outbreaks of hemorrhagic fever originated as laboratory-acquired human infections from grivets (Chlorocebus aethiops) imported from Uganda2,<a data-track="click" data-track-action="reference anchor" data-track-label="link" data-test="citation-ref" aria-label="Reference 3" title="Ristanović, E. S., Kokoškov, N. S., Crozier, I., Kuhn, J. H. & Gligić, A. S. A forgotten episode of marburg virus disease: Belgrade,