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

Liu Y,Hill MG,Klose T,Chen Z,Watters K,Bochkov YA,Jiang W,Palmenberg AC,Rossmann MG

doi

10.1073/pnas.1606595113

subject

Has Abstract

pub_date

2016-08-09 00:00:00

pages

8997-9002

issue

32

eissn

0027-8424

issn

1091-6490

pii

1606595113

journal_volume

113

pub_type

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