7C5Z

Crystal structure of spring viremia of carp virus phosphoprotein central domain

7C5Z の概要

• エントリーDOI: 10.2210/pdb7c5z/pdb
• 分子名称: Phosphoprotein (2 entities in total)
• 機能のキーワード: svcv, p protein, central domain, dimer, viral protein
• 由来する生物種: Spring viremia of carp virus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19536.87

構造登録者

Wang, Z.X.,Guan, H.X.,Ouyang, S.Y.,Zhang, Y.A. (登録日: 2020-05-21, 公開日: 2020-08-05, 最終更新日: 2024-11-20)

主引用文献

Wang, Z.X.,Liu, S.B.,Guan, H.,Lu, L.F.,Tu, J.G.,Ouyang, S.,Zhang, Y.A.
Structural and Functional Characterization of the Phosphoprotein Central Domain of Spring Viremia of Carp Virus.
J.Virol., 94:-, 2020

PubMed Abstract: Spring viremia of carp virus (SVCV) is a highly pathogenic 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) of SVCV (SVCV). The P monomer consists of two β sheets, an α helix, and another two β sheets. Two P monomers pack together through their hydrophobic surfaces to form a dimer. The mutations of residues on the hydrophobic surfaces of P disrupt the dimer formation to different degrees and affect the expression of host IFN consistently. Therefore, the oligomeric state formation of the P protein of SVCV is an important mechanism to negatively regulate host IFN response. 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 in immunosuppression. Here, we present the crystal structure of SVCV A new mechanism of immune evasion is clarified by exploring the relationship between SVCV 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.

PubMed: 32434890
DOI: 10.1128/JVI.00855-20

実験手法

X-RAY DIFFRACTION (1.5 Å)