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Atomic structure of a rhinovirus C, a virus species linked to severe childhood asthma

Significance The recently identified rhinovirus C (RV-C) species of picornaviruses might be associated with more severe respiratory infections than other rhinoviruses in children. The RV-C have been linked to 50–85% of hospital-level childhood asthma exacerbations that can lead to significant adult respiratory problems. However, there are currently no effective antiviral treatments or vaccines available. Using cryoelectron microscopy, we have determined the atomic structures of the full virion and native empty particle (NEP) of a cell-adapted RV-C strain. The structures highlight novel immunogenic sites on the virus surface, a probable binding site for the RV-C receptor, molecular determinants of antiviral resistance, and the rationale of utilizing NEPs as vaccine candidates. These results provide the basis for designing antiviral therapeutics and vaccines. 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.