Crystal structure of the dimerized of porcine circovirus type II replication-related protein Rep'
Crystal structure of the dimerized of porcine circovirus type II replication-related protein Rep'
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DOI：
10.1002/prot.26498
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发表时间：
2023-05-12
影响因子：
2.9
通讯作者：
Song, Yunfeng
中科院分区：
文献类型：
--
作者：
Guan, Shuaiyin;Tian, Ang;Song, Yunfeng
猪圆环病毒2型（Porcine Circovirus type 2，PCV 2）可引起猪圆环病毒相关病（Porcine Circovirus associated disease，PCVAD），每年给全球养猪业造成重大经济损失。没有有效的抗病毒药物用于控制和治疗PCV 2，预防主要通过接种疫苗获得。PCV 2基因组通过涉及Rep和Rep '的滚环复制（RCR）机制进行复制，因此分析Rep和Rep'的整体结构将有助于我们更好地理解PCV 2的复制过程。然而，目前还没有关于Rep'和Rep的完整结构的报道，这严重阻碍了对病毒复制的研究。用X-射线衍射法对Rep'二聚体的结构进行了解析。结构分析表明，Rep'是由C-末端结构域相互作用形成的二聚体。两个Rep'形成带正电荷的沟，其可能在dsDNA的病毒结合中起重要作用。总之，这项研究有助于了解病毒的复制过程，也可能为抗病毒药物的开发提供新的见解。
Porcine circovirus type 2 (PCV2) can cause porcine circovirus-associated disease (PCVAD), which causes significant economic losses to the global pig industry annually. There are no effective antiviral drugs used to control and treat PCV2, and prevention is mainly obtained through vaccination. PCV2 genome replicates through the rolling circle replication (RCR) mechanism involving Rep and Rep', so analyzing the holistic structure of Rep and Rep' will help us better understand the replication process of PCV2. However, there are no reports on the integral structure of Rep' and Rep, which seriously hinders the research of the viral replication. By using the x-ray diffraction method, the structure of the Rep' dimer was resolved by us in this study. Structural analysis revealed that Rep' is a dimer formed by the interaction of the C-terminal domain. The two Rep' form a positively charged groove, which may play an essential role in the viral binding of dsDNA. Together, this study help to under-stand the replication process of the virus and may also provide new insights into the development of antiviral drugs.