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TitleCryo-EM of human rhinovirus reveals capsid-RNA duplex interactions that provide insights into virus assembly and genome uncoating.
Journal, issue, pagesCommun Biol, Vol. 7, Issue 1, Page 1501, Year 2024
Publish dateNov 13, 2024
AuthorsDavid Gil-Cantero / Carlos P Mata / Luis Valiente / Alicia Rodríguez-Huete / Alejandro Valbuena / Reidun Twarock / Peter G Stockley / Mauricio G Mateu / José R Castón /
PubMed AbstractThe cryo-EM structure of the human rhinovirus B14 determined in this study reveals 13-bp RNA duplexes symmetrically bound to regions around each of the 30 two-fold axes in the icosahedral viral ...The cryo-EM structure of the human rhinovirus B14 determined in this study reveals 13-bp RNA duplexes symmetrically bound to regions around each of the 30 two-fold axes in the icosahedral viral capsid. The RNA duplexes (~12% of the ssRNA genome) define a quasi-dodecahedral cage that line a substantial part of the capsid interior surface. The RNA duplexes establish a complex network of non-covalent interactions with pockets in the capsid inner wall, including coulombic interactions with a cluster of basic amino acid residues that surround each RNA duplex. A direct comparison was made between the cryo-EM structure of RNA-filled virions and that of RNA-free (empty) capsids that resulted from genome release from a small fraction of viruses. The comparison reveals that some specific residues involved in capsid-duplex RNA interactions in the virion undergo remarkable conformational rearrangements upon RNA release from the capsid. RNA release is also associated with the asynchronous opening of channels at the 30 two-fold axes. The results provide further insights into the molecular mechanisms leading to assembly of rhinovirus particles and their genome uncoating during infection. They may also contribute to development of novel antiviral strategies aimed at interfering with viral capsid-genome interactions during the infectious cycle.
External linksCommun Biol / PubMed:39537894 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 3.8 Å
Structure data

17780

8pnb

EMDB-17780, PDB-8pnb:
HRV empty capsid
Method: EM (single particle) / Resolution: 3.8 Å

17781

8pnf

EMDB-17781, PDB-8pnf:
HRV B14 virion proteins
Method: EM (single particle) / Resolution: 2.9 Å

Source
  • rhinovirus b14
KeywordsVIRUS / cryo-EM / HRV-B14 / SsRNA virus / capsid / HRV B14 / dsRNA virus

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