Summary for 8PNB
| Entry DOI | 10.2210/pdb8pnb/pdb |
| EMDB information | 17780 |
| Descriptor | Capsid protein VP1, Capsid protein VP2, Genome polyprotein (3 entities in total) |
| Functional Keywords | cryo-em, hrv-b14, ssrna virus, capsid, virus |
| Biological source | rhinovirus B14 More |
| Total number of polymer chains | 3 |
| Total formula weight | 80373.92 |
| Authors | Gil-Cantero, D.,Mata, C.P.,Mateu, M.G.,Caston, J.R. (deposition date: 2023-06-30, release date: 2024-11-20, Last modification date: 2025-07-02) |
| Primary citation | Gil-Cantero, D.,Mata, C.P.,Valiente, L.,Rodriguez-Huete, A.,Valbuena, A.,Twarock, R.,Stockley, P.G.,Mateu, M.G.,Caston, J.R. Cryo-EM of human rhinovirus reveals capsid-RNA duplex interactions that provide insights into virus assembly and genome uncoating. Commun Biol, 7:1501-1501, 2024 Cited by PubMed Abstract: 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. PubMed: 39537894DOI: 10.1038/s42003-024-07213-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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