Investigating the mechanism of Echovirus 30 cell invasion

Figures

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  Figure 1. (A) Schematic representation of the E30 gene structure. The uORF is on the left. The 5’ end of the E30 genome is covalently linked to a viral protein genome-linked (VPg). (B) The first line indicates the surface of E30 F-, E-, and A-particles along the icosahedral twofold axes. The A-particle forms perforations at the icosahedral two-fold axes. The surfaces are rainbow-colored by radius from red through indigo, green, and yellow to blue, which correspond to 120, 135, 145, 155, and 165 nm. The second line represents thin slices of the central sections of each particle; they use the same color scheme.

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  Figure 2. (A) Surface of the protein structures of E30 F-, E-, and A-particles (VP0, orange red; VP1, blue; VP2, indigo; VP3, green; VP4, red), The F-particle has a hydrophobic pocket containing a pocket factor in VP1, labeled with magenta. And the canyon region is in VP1. (B) Residues at the main E30-DAF (left) and E30-FcRn (right) interfaces. The side or main chains involved in mutual interactions are shown as sticks. The hydrogen bonds are shown as yellow dashed lines.

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  Figure 3. Schematic of the mechanism by which E30 invades the RD cell. Lipid raft proteins mediate endocytosis when E30 interacts with DAF on the surface of the cell. The queried pathway suggests it is unclear whether αvβ3 or FcRn alone or in association with DAF mediates the same process. After entering the cells, E30 decapitates in the endosome via FcRn, causing conformational changes in the virus and the release of genetic material. This genetic material is then replicated by the replication organelle (RO), where the translation polyprotein further hydrolyzes to a replication protein and capsid protein. Of these, the former may participate in the replication process, and the latter further processes and assembles the genetic material into new virions, which are released from the cells in a lytic or non-lytic pathway.