Structural and Functional Characterization of the Phosphoprotein Central Domain of Spring Viremia of Carp Virus.

ABSTRACT: Spring viremia of carp virus (SVCV) is a highly pathogenic Vesiculovirus in the common carp. The phosphoprotein (P protein) of SVCV is a multifunctional protein that acts as a polymerase cofactor and an antagonist of cellular interferon (IFN) response. Here, we report the 1.5-Å-resolution crystal structure of the P protein central domain (P_CD) of SVCV (SVCV_PCD). The P_CD monomer consists of two β sheets, an α helix, and another two β sheets. Two P_CD monomers pack together through their hydrophobic surfaces to form a dimer. The mutations of residues on the hydrophobic surfaces of P_CD disrupt the dimer formation to different degrees and affect the expression of host IFN consistently. Therefore, the oligomeric state formation of the

SUBMITTER: Wang ZX 

PROVIDER: S-EPMC7375382 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature