Cryoelectron microscopic structure of the nucleoprotein-RNA complex of the European filovirus, Lloviu virus

Lloviu virus (LLOV) is a novel filovirus detected in Schreiber's bats in Europe. The isolation of the infectious LLOV from bats has raised public health concerns. However, the virological and molecular characteristics of LLOV remain largely unknown. The nucleoprotein (NP) of LLOV encapsidates the viral genomic RNA to form a helical NP-RNA complex, which acts as a scaffold for nucleocapsid formation and de novo viral RNA synthesis. In this study, using single-particle cryoelectron microscopy, we determined two structures of the LLOV NP-RNA helical complex, comprising a full-length and a C-terminally truncated NP. The two helical structures were identical, demonstrating that the N-terminal region determines the helical arrangement of the NP. The LLOV NP-RNA protomers displayed a structure similar to that in the Ebola and Marburg virus, but the spatial arrangements in the helix differed. Structure-based mutational analysis identified amino acids involved in the helical assembly and viral RNA synthesis. These structures advance our understanding of the filovirus nucleocapsid formation and provide a structural basis for the development of antifiloviral therapeutics.

Automated summary

In this study, the structure of the Lloviu virus nucleoprotein-RNA helical complex was determined using cryoelectron microscopy. The results showed that the N-terminal region of the nucleoprotein determines the helical arrangement, and identified amino acids involved in helical assembly and viral RNA synthesis. These findings advance our understanding of filovirus nucleocapsid formation and have implications for antiviral therapeutics development.