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

Abstract

SVCV can cause spring viremia of carp with up to 90% lethality, and it is the homologous virus of the notorious vesicular stomatitis virus (VSV). There are currently no drugs that effectively cure this disease. P proteins of negative-strand RNA viruses (NSVs) play an essential role in many steps during the replication cycle and an additional role in immunosuppression as a cofactor. All P proteins of NSVs are oligomeric, but the studies on the role of this oligomerization mainly focus on the process of virus transcription or replication, and there are few studies on the role of P CD in immunosuppression. Here, we present the crystal structure of SVCV PCD . A new mechanism of immune evasion is clarified by exploring the relationship between SVCV PCD and host IFN response from a structural biology point of view. These findings may provide more accurate target sites for drug design against SVCV and provide new insights into the function of NSV PCD .