非洲猪瘟病毒 CP312R 蛋白的结构见解。

Structural insights into the CP312R protein of the African swine fever virus.

机构信息

Provincial University Key Laboratory of Cellular Stress Response and Metabolic Regulation & Fujian Key Laboratory of Developmental and Neural Biology, College of Life Sciences, Fujian Normal University, Fuzhou, 350117, China.

MOE Joint International Research Laboratory of Animal Health and Food Safety, College of Veterinary Medicine, Nanjing Agricultural University, Nanjing, Jiangsu Province, China.

出版信息

Biochem Biophys Res Commun. 2022 Oct 8;624:68-74. doi: 10.1016/j.bbrc.2022.07.091. Epub 2022 Jul 31.

DOI:10.1016/j.bbrc.2022.07.091

PMID:35933928

Abstract

African swine fever (ASF) is a lethal hemorrhagic disease that affects domestic pigs and wild boars. There is no medication available for ASF to date. The ability to mount antigen-specific responses to viral vectored CP312R makes it a crucial potential target for designing vaccines or drugs. This study determined the crystal structure of ASFV CP312R at 2.32 Å and found it to be a monomer with a single-stranded DNA binding core domain with a clear five-strands β-barrel OB-fold architecture. Electrophoretic mobility shift assay and size-exclusion chromatography characterization assay further confirmed the single-stranded DNA (ssDNA)-binding property of ASFV CP312R. This study revealed the structure and preliminary ssDNA interaction mechanisms of ASFV CP312R, providing new clues for developing new antiviral strategies.

摘要

非洲猪瘟（ASF）是一种致命的出血性疾病，会影响家猪和野猪。迄今为止，尚无针对 ASF 的药物。目前，能够对病毒载体 CP312R 产生抗原特异性反应，使其成为设计疫苗或药物的重要潜在目标。本研究确定了 ASFV CP312R 的 2.32 Å 晶体结构，发现它是一个单体，具有单链 DNA 结合核心域，具有清晰的五链 β-桶 OB 折叠结构。电泳迁移率变动分析和大小排阻色谱分析进一步证实了 ASFV CP312R 的单链 DNA（ssDNA）结合特性。本研究揭示了 ASFV CP312R 的结构和初步的 ssDNA 相互作用机制，为开发新的抗病毒策略提供了新的线索。