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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/E5D8F2_9ENTO E5D8F2_9ENTO] | | [https://www.uniprot.org/uniprot/E5D8F2_9ENTO E5D8F2_9ENTO] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| 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.
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| 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<ref>PMID:27511920</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 5k0u" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </SX> | | </SX> |
