title: Atomic structure of a rhinovirus C, a virus species linked to severe childhood asthma.
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.
authors: Department of Biological Sciences, Purdue University, West Lafayette, IN 47907;
authors: Yue
authors: Y
authors: Liu
authors: Institute for Molecular Virology, University of Wisconsin, Madison, WI 53706;
authors: Marchel G
authors: MG
authors: Hill
authors: Department of Biological Sciences, Purdue University, West Lafayette, IN 47907;
authors: Thomas
authors: T
authors: Klose
authors: Department of Biological Sciences, Purdue University, West Lafayette, IN 47907;
authors: Zhenguo
authors: Z
authors: Chen
authors: Institute for Molecular Virology, University of Wisconsin, Madison, WI 53706;
authors: Kelly
authors: K
authors: Watters
authors: Department of Pediatrics, School of Medicine and Public Health, University of Wisconsin, Madison, WI 53706.
authors: Yury A
authors: YA
authors: Bochkov
authors: Department of Biological Sciences, Purdue University, West Lafayette, IN 47907;
authors: Wen
authors: W
authors: Jiang
authors: Institute for Molecular Virology, University of Wisconsin, Madison, WI 53706; mr@purdue.edu acpalmen@wisc.edu.
authors: Ann C
authors: AC
authors: Palmenberg
authors: Department of Biological Sciences, Purdue University, West Lafayette, IN 47907; mr@purdue.edu acpalmen@wisc.edu.
authors: Michael G
authors: MG
authors: Rossmann
mesh_terms: D001249:Asthma / Q000209:etiology* / Q000821:virology; D017124:Conserved Sequence; D020285:Cryoelectron Microscopy; D004770:Enterovirus / Q000648:ultrastructure*; D006031:Glycosylation; D006801:Humans; D011991:Receptors, Virus / Q000737:chemistry; D014771:Virion / Q000648:ultrastructure*
chemical_list: D011991:Receptors, Virus
keywords: asthma; atomic structure; cryoelectron microscopy; rhinovirus C