7QB5
Coxsackievirus A24v (CVA24v) in complex with a dimeric C2-C9-linked sialic acid inhibitor
This is a non-PDB format compatible entry.
Summary for 7QB5
| Entry DOI | 10.2210/pdb7qb5/pdb |
| Descriptor | Capsid protein VP1, Capsid protein VP2, Capsid protein VP3, ... (9 entities in total) |
| Functional Keywords | coxsackievirus a24v, cva24v, sialic acid based inhibitor, virus |
| Biological source | Coxsackievirus A24 More |
| Total number of polymer chains | 4 |
| Total formula weight | 98882.14 |
| Authors | Zocher, G.,Stehle, T. (deposition date: 2021-11-18, release date: 2022-05-18, Last modification date: 2024-01-31) |
| Primary citation | Johansson, E.,Caraballo, R.,Zocher, G.,Mistry, N.,Arnberg, N.,Stehle, T.,Elofsson, M. Exploring divalent conjugates of 5- N -acetyl-neuraminic acid as inhibitors of coxsackievirus A24 variant (CVA24v) transduction. Rsc Adv, 12:2319-2331, 2022 Cited by PubMed Abstract: Coxsackievirus A24 variant (CVA24v) is responsible for several outbreaks and two pandemics of the highly contagious eye infection acute hemorrhagic conjunctivitis (AHC). Currently, neither prevention (vaccines) nor treatments (antivirals) are available for combating this disease. CVA24v attaches to cells by binding Neu5Ac-containing glycans on the surface of cells which facilitates entry. Previously, we have demonstrated that pentavalent Neu5Ac conjugates attenuate CVA24v infection of human corneal epithelial (HCE) cells. In this study, we report on the structure-based design of three classes of divalent Neu5Ac conjugates, with varying spacer lengths, and their effect on CVA24v transduction in HCE cells. In relative terms, the most efficient class of divalent Neu5Ac conjugates are more efficient than the pentavalent Neu5Ac conjugates previously reported. PubMed: 35425270DOI: 10.1039/d1ra08968d PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.728 Å) |
Structure validation
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