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Publication Abstract from PubMed

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.

Atomic structure of a rhinovirus C, a virus species linked to severe childhood asthma.,Liu Y, Hill MG, Klose T, Chen Z, Watters K, Bochkov YA, Jiang W, Palmenberg AC, Rossmann MG Proc Natl Acad Sci U S A. 2016 Aug 9;113(32):8997-9002. doi:, 10.1073/pnas.1606595113. Epub 2016 Jul 11. PMID:27511920^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.