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.
journal_name
Proc Natl Acad Sci U S Aauthors
Liu Y,Hill MG,Klose T,Chen Z,Watters K,Bochkov YA,Jiang W,Palmenberg AC,Rossmann MGdoi
10.1073/pnas.1606595113subject
Has Abstractpub_date
2016-08-09 00:00:00pages
8997-9002issue
32eissn
0027-8424issn
1091-6490pii
1606595113journal_volume
113pub_type
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