The VP1/2 Protein of a New Recombinant PRV Strain Promotes the Infectivity and Pathogenicity of PRV in Northeastern China

Figure 4

According to the differences in amino acid protein three-dimensional structure comparison. (a) For OBP protein (UL9) 3D model alignment, the deletion of three amino acids of AGA at 254–255 aa resulted in subsequent helical alterations in the isolates compared with other strains. (b) For the 3D model alignment of the AN protein (UL12), the deletion of phenylalanine at 410–411 aa in the isolates resulted in the production of specific bumps in the protein compared with other strains. (c) Comparison of the 3D model of UL17 protein showed that the deletion of alanine at 248–249 aa shifted but did not change the structure of the isolate compared with other strains. (d) 2,310–2,530 aa range of the VP1/2 protein (UL36) was simulated, and the protein tertiary structure of the isolates was found to have lost an alpha helix at 77–92 aa and added an alpha helix at 141–160 aa compared to other strains. In addition, four additional alpha helices were lost within this simulation range due to generalized mutations in the isolates.

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