Figure 2

Structural modeling and identification of ChiEV-A71 VLPs.
(A) Structural modeling using the SWISS-MODEL server (http://swissmodel.expasy.org). A cartoon representation of a protomer with VP1, VP2, VP3 and SP70 epitope colored in magenta, yellow, cyan and blue, respectively, showed that the replaced SP70 peptide from CVA16 protruded from the natural VP1 proteins. (B) A cartoon representation of the capsid with VP1, VP2, VP3 and SP70 epitope colored in magenta, yellow, cyan and blue, respectively. The 60 copies of CVA16-SP70 peptides were predicted to be uniformly displayed on the surface of EV-A71 VLP without affecting the original structure. (C) Electron micrograph of negatively stained ChiEV-A71 VLPs. These VLPs are about 30 nm in diameter and are morphologically similar to EV-A71-VLPs. ELISA of purified ChiEV-A71 VLPs was performed using polyclonal antibody against CVA16-SP70 peptide (D) and monoclonal antibody targeting EV-A71-SP70 epitope (E), respectively. Yeast antigen was control. The cut-off for the ELISA is shown by a dotted line. **P < 0.01 for ChiEV-A71 vs. EV-A71 group, by one-way ANOVA.