Author:
Liu Yue,Hill Marchel G.,Klose Thomas,Chen Zhenguo,Watters Kelly,Bochkov Yury A.,Jiang Wen,Palmenberg Ann C.,Rossmann Michael G.
Abstract
Isolates of rhinovirus C (RV-C), a recently identifiedEnterovirus(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.
Funder
HHS | National Institutes of Health
Publisher
Proceedings of the National Academy of Sciences
Cited by
63 articles.
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