Summary for 6X2I
| Entry DOI | 10.2210/pdb6x2i/pdb |
| EMDB information | 22008 22010 |
| Descriptor | VP2 (1 entity in total) |
| Functional Keywords | icosahedral capsid, cutavirus, cuv, virus, protoparvovirus |
| Biological source | Cutavirus |
| Total number of polymer chains | 60 |
| Total formula weight | 3675152.82 |
| Authors | Mietzsch, M.,Agbandje-McKenna, M. (deposition date: 2020-05-20, release date: 2020-07-01, Last modification date: 2025-05-21) |
| Primary citation | Mietzsch, M.,McKenna, R.,Vaisanen, E.,Yu, J.C.,Ilyas, M.,Hull, J.A.,Kurian, J.,Smith, J.K.,Chipman, P.,Lasanajak, Y.,Smith, D.,Soderlund-Venermo, M.,Agbandje-McKenna, M. Structural Characterization of Cuta- and Tusavirus: Insight into Protoparvoviruses Capsid Morphology. Viruses, 12:-, 2020 Cited by PubMed Abstract: Several members of the genus, capable of infecting humans, have been recently discovered, including cutavirus (CuV) and tusavirus (TuV). To begin the characterization of these viruses, we have used cryo-electron microscopy and image reconstruction to determine their capsid structures to ~2.9 Å resolution, and glycan array and cell-based assays to identify glycans utilized for cellular entry. Structural comparisons show that the CuV and TuV capsids share common features with other parvoviruses, including an eight-stranded anti-parallel β-barrel, depressions at the icosahedral 2-fold and surrounding the 5-fold axes, and a channel at the 5-fold axes. However, the viruses exhibit significant topological differences in their viral protein surface loops. These result in three separated 3-fold protrusions, similar to the bufaviruses also infecting humans, suggesting a host-driven structure evolution. The surface loops contain residues involved in receptor binding, cellular trafficking, and antigenic reactivity in other parvoviruses. In addition, terminal sialic acid was identified as the glycan potentially utilized by both CuV and TuV for cellular entry, with TuV showing additional recognition of poly-sialic acid and sialylated Lewis X (sLeXLeXLeX) motifs reported to be upregulated in neurotropic and cancer cells, respectively. These structures provide a platform for annotating the cellular interactions of these human pathogens. PubMed: 32560452DOI: 10.3390/v12060653 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.87 Å) |
Structure validation
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