Unknown

Dataset Information

0

High resolution cryo-EM structure of the helical RNA-bound Hantaan virus nucleocapsid reveals its assembly mechanisms.


ABSTRACT: Negative-strand RNA viruses condense their genome into helical nucleocapsids that constitute essential templates for viral replication and transcription. The intrinsic flexibility of nucleocapsids usually prevents their full-length structural characterisation at high resolution. Here, we describe purification of full-length recombinant metastable helical nucleocapsid of Hantaan virus (Hantaviridae family, Bunyavirales order) and determine its structure at 3.3 Å resolution by cryo-electron microscopy. The structure reveals the mechanisms of helical multimerisation via sub-domain exchanges between protomers and highlights nucleotide positions in a continuous positively charged groove compatible with viral genome binding. It uncovers key sites for future structure-based design of antivirals that are currently lacking to counteract life-threatening hantavirus infections. The structure also suggests a model of nucleoprotein-polymerase interaction that would enable replication and transcription solely upon local disruption of the nucleocapsid.

SUBMITTER: Arragain B 

PROVIDER: S-EPMC6365055 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

High resolution cryo-EM structure of the helical RNA-bound Hantaan virus nucleocapsid reveals its assembly mechanisms.

Arragain Benoît B   Reguera Juan J   Desfosses Ambroise A   Gutsche Irina I   Schoehn Guy G   Malet Hélène H  

eLife 20190114


Negative-strand RNA viruses condense their genome into helical nucleocapsids that constitute essential templates for viral replication and transcription. The intrinsic flexibility of nucleocapsids usually prevents their full-length structural characterisation at high resolution. Here, we describe purification of full-length recombinant metastable helical nucleocapsid of Hantaan virus (<i>Hantaviridae</i> family, <i>Bunyavirales</i> order) and determine its structure at 3.3 Å resolution by cryo-e  ...[more]

Similar Datasets

| S-EPMC4682053 | biostudies-literature
| S-EPMC8689349 | biostudies-literature
| S-EPMC10444854 | biostudies-literature
| S-EPMC2689313 | biostudies-literature
| S-EPMC6905873 | biostudies-literature
| S-EPMC7316398 | biostudies-literature
| S-EPMC10657434 | biostudies-literature
| EMPIAR-11540 | biostudies-other
| S-EPMC8860596 | biostudies-literature
| S-EPMC6478846 | biostudies-literature