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

Yue Liu, Marchel G. Hill, Thomas Klose, Zhenguo Chen, Kelly Watters, Yury A. Bochkov, Wen Jiang, Ann C. Palmenberg, Michael G. Rossmann

Research output: Contribution to journalArticlepeer-review

53 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)8997-9002
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number32
StatePublished - Aug 9 2016


  • Rhinovirus c|cryoelectron microscopy|atomic structure|asthma

ASJC Scopus subject areas

  • General


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