5K0U

CryoEM structure of the full virion of a human rhinovirus C

Summary for 5K0U

• Entry DOI: 10.2210/pdb5k0u/pdb
• Related: 5JZG
• EMDB information: 8184 8189
• Descriptor: Capsid protein VP1, Capsid protein VP3, Capsid protein VP2, ... (5 entities in total)
• Functional Keywords: virus, jelly roll
• Biological source: Rhinovirus C; More
• Total number of polymer chains: 4
• Total formula weight: 94033.08

Authors

Liu, Y.,Hill, M.G.,Klose, T.,Chen, Z.,Watters, K.E.,Jiang, W.,Palmenberg, A.C.,Rossmann, M.G. (deposition date: 2016-05-17, release date: 2016-07-13, Last modification date: 2024-03-06)

Primary citation

Liu, Y.,Hill, M.G.,Klose, T.,Chen, Z.,Watters, K.,Bochkov, Y.A.,Jiang, W.,Palmenberg, A.C.,Rossmann, M.G.
Atomic structure of a rhinovirus C, a virus species linked to severe childhood asthma.
Proc.Natl.Acad.Sci.USA, 113:8997-9002, 2016

PubMed Abstract: Isolates of rhinovirus C (RV-C), a recently identified Enterovirus (EV) species, are the causative agents of severe respiratory infections among children and are linked to childhood asthma exacerbations. The RV-C have been refractory to structure determination because they are difficult to propagate in vitro. Here, we report the cryo-EM atomic structures of the full virion and native empty particle (NEP) of RV-C15a. The virus has 60 "fingers" on the virus outer surface that probably function as dominant immunogens. Because the NEPs also display these fingers, they may have utility as vaccine candidates. A sequence-conserved surface depression adjacent to each finger forms a likely binding site for the sialic acid on its receptor. The RV-C, unlike other EVs, are resistant to capsid-binding antiviral compounds because the hydrophobic pocket in VP1 is filled with multiple bulky residues. These results define potential molecular determinants for designing antiviral therapeutics and vaccines.

PubMed: 27511920
DOI: 10.1073/pnas.1606595113

Experimental method

ELECTRON MICROSCOPY (2.79 Å)