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TitleHigh resolution cryo-EM structure of the helical RNA-bound Hantaan virus nucleocapsid reveals its assembly mechanisms.
Journal, issue, pagesElife, Vol. 8, Year 2019
Publish dateJan 14, 2019
AuthorsBenoît Arragain / Juan Reguera / Ambroise Desfosses / Irina Gutsche / Guy Schoehn / Hélène Malet /
PubMed AbstractNegative-strand RNA viruses condense their genome into helical nucleocapsids that constitute essential templates for viral replication and transcription. The intrinsic flexibility of nucleocapsids ...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 ( family, 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.
External linksElife / PubMed:30638449 / PubMed Central
MethodsEM (helical sym.)
Resolution3.3 Å
Structure data

0333

6i2n

EMDB-0333, PDB-6i2n:
Helical RNA-bound Hantaan virus nucleocapsid
Method: EM (helical sym.) / Resolution: 3.3 Å

Source
  • hantaan orthohantavirus
  • spodoptera frugiperda (fall armyworm)
KeywordsVIRAL PROTEIN / Nucleoprotein / Nucleocapsid / RNA-binding

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