State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health, School of Life Sciences, Xiamen University, Xiamen, 361102, China.
National Institute of Diagnostics and Vaccine Development in Infectious Diseases, Xiamen University, Xiamen, 361102, China.
Nat Commun. 2022 Mar 22;13(1):1533. doi: 10.1038/s41467-022-29250-3.
Pseudorabies virus (PRV) is a major etiological agent of swine infectious diseases and is responsible for significant economic losses in the swine industry. Recent data points to human viral encephalitis caused by PRV infection, suggesting that PRV may be able to overcome the species barrier to infect humans. To date, there is no available therapeutic for PRV infection. Here, we report the near-atomic structures of the PRV A-capsid and C-capsid, and illustrate the interaction that occurs between these subunits. We show that the C-capsid portal complex is decorated with capsid-associated tegument complexes. The PRV capsid structure is highly reminiscent of other α-herpesviruses, with some additional structural features of β- and γ-herpesviruses. These results illustrate the structure of the PRV capsid and elucidate the underlying assembly mechanism at the molecular level. This knowledge may be useful for the development of oncolytic agents or specific therapeutics against this arm of the herpesvirus family.
伪狂犬病病毒（PRV）是一种主要的猪传染病病原，给养猪业造成了巨大的经济损失。最近的数据表明，PRV 感染可引起人类病毒性脑炎，提示 PRV 可能能够突破种间屏障感染人类。迄今为止，尚无针对 PRV 感染的有效治疗方法。在这里，我们报告了 PRV A 衣壳和 C 衣壳的近原子结构，并阐明了这些亚基之间的相互作用。我们发现 C 衣壳的门复合结构上装饰有衣壳相关的被膜复合物。PRV 衣壳结构与其他α疱疹病毒高度相似，具有β和γ疱疹病毒的一些额外结构特征。这些结果说明了 PRV 衣壳的结构，并阐明了分子水平上的基本组装机制。这些知识可能有助于开发针对疱疹病毒家族这一支的溶瘤剂或特异性治疗药物。
