SNAP output for PDB entry 7yg7 [SNAP web server]

PDB-id

7yg7; SNAP-derived features in text and JSON formats; DNAproDB

Class

virus like particle-RNA

Method

cryo-EM (3.7 Å)

Summary

Structure of the spring viraemia of carp virus ribonucleoprotein complex

Reference

Wang ZX, Liu B, Yang T, Yu D, Zhang C, Zheng L, Xie J, Liu B, Liu M, Peng H, Lai L, Ouyang Q, Ouyang S, Zhang YA (2023): "Structure of the Spring Viraemia of Carp Virus Ribonucleoprotein Complex Reveals Its Assembly Mechanism and Application in Antiviral Drug Screening." J.Virol., 97, e0182922. doi: 10.1128/jvi.01829-22.

Abstract

Spring viremia of carp virus (SVCV) is a highly pathogenic Vesiculovirus infecting the common carp, yet neither a vaccine nor effective therapies are available to treat spring viremia of carp (SVC). Like all negative-sense viruses, SVCV contains an RNA genome that is encapsidated by the nucleoprotein (N) in the form of a ribonucleoprotein (RNP) complex, which serves as the template for viral replication and transcription. Here, the three-dimensional (3D) structure of SVCV RNP was resolved through cryo-electron microscopy (cryo-EM) at a resolution of 3.7 Å. RNP assembly was stabilized by N and C loops; RNA was wrapped in the groove between the N and C lobes with 9 nt nucleotide per protomer. Combined with mutational analysis, our results elucidated the mechanism of RNP formation. The RNA binding groove of SVCV N was used as a target for drug virtual screening, and it was found suramin had a good antiviral effect. This study provided insights into RNP assembly, and anti-SVCV drug screening was performed on the basis of this structure, providing a theoretical basis and efficient drug screening method for the prevention and treatment of SVC.