8R6X
Cryo-EM structure of a coxsackievirus A6 virus-like particle
Summary for 8R6X
| Entry DOI | 10.2210/pdb8r6x/pdb |
| EMDB information | 18968 |
| Descriptor | Genome polyprotein (3 entities in total) |
| Functional Keywords | coxsackievirus, virus-like particle, virus like particle |
| Biological source | Coxsackievirus A6 More |
| Total number of polymer chains | 3 |
| Total formula weight | 95342.67 |
| Authors | Giannopoulou, E.A.,Jakobi, A.J. (deposition date: 2023-11-23, release date: 2024-10-16, Last modification date: 2025-02-12) |
| Primary citation | Kuijpers, L.,Giannopoulou, E.A.,Feng, Y.,van den Braak, W.,Freydoonian, A.,Ramlal, R.,Meiring, H.,Solano, B.,Roos, W.H.,Jakobi, A.J.,van der Pol, L.A.,Dekker, N.H. Enterovirus-like particles encapsidate RNA and exhibit decreased stability due to lack of maturation. Plos Pathog., 21:e1012873-e1012873, 2025 Cited by PubMed Abstract: To counteract hand, foot, and mouth disease-causing viruses such as enterovirus A71 and coxsackievirus A6, virus-like particles (VLPs) have emerged as a leading contender for the development of a multivalent vaccine. However, VLPs have shown rapid conversion from a highly immunogenic state to a less immunogenic state and low particle integrity lifetimes compared to inactivated virus vaccines, thus raising concerns about their overall stability. Here, we produce VLPs to investigate capsid stability using cryogenic electron microscopy (cryo-EM), mass spectrometry (MS), biochemical assays, and atomic force microscopy (AFM). In contrast to prior studies and prevailing hypotheses, we show that insect-cell produced enterovirus VLPs include encapsidated RNA fragments with viral protein coding sequences. Our integrated approach reveals that CVA6 VLPs do not undergo viral maturation, in contrast to virions; that they can encapsidate RNA fragments, similarly to virions; and that despite the latter, they are more brittle than virions. Interestingly, this indicates that CVA6 VLP stability is more affected by lack of viral maturation than the presence of RNA. Our study highlights how the development of VLPs as vaccine candidates should encompass probing for unwanted (viral) RNA content and establishing control of their maturation to enhance stability. PubMed: 39903789DOI: 10.1371/journal.ppat.1012873 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.15 Å) |
Structure validation
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