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-Structure paper
Title | Atomic structure of a rhinovirus C, a virus species linked to severe childhood asthma. |
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Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 113, Issue 32, Page 8997-9002, Year 2016 |
Publish date | Aug 9, 2016 |
Authors | Yue Liu / Marchel G Hill / Thomas Klose / Zhenguo Chen / Kelly Watters / Yury A Bochkov / Wen Jiang / Ann C Palmenberg / Michael G Rossmann / |
PubMed 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 ...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. |
External links | Proc Natl Acad Sci U S A / PubMed:27511920 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.79 - 3.16 Å |
Structure data | |
Chemicals | ChemComp-HOH: |
Source |
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Keywords | VIRUS / jelly roll |