Department of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut 06269, USA; email:
Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.
Annu Rev Virol. 2019 Sep 29;6(1):141-160. doi: 10.1146/annurev-virology-092818-015819. Epub 2019 Jul 23.
Tailed, double-stranded DNA bacteriophages provide a well-characterized model system for the study of viral assembly, especially for herpesviruses and adenoviruses. A wealth of genetic, structural, and biochemical work has allowed for the development of assembly models and an understanding of the DNA packaging process. The portal complex is an essential player in all aspects of bacteriophage and herpesvirus assembly. Despite having low sequence similarity, portal structures across bacteriophages share the portal fold and maintain a conserved function. Due to their dynamic role, portal proteins are surprisingly plastic, and their conformations change for each stage of assembly. Because the maturation process is dependent on the portal protein, researchers have been working to validate this protein as a potential antiviral drug target. Here we review recent work on the role of portal complexes in capsid assembly, including DNA packaging, as well as portal ring assembly and incorporation and analysis of portal structures.
有尾、双链 DNA 噬菌体为病毒组装的研究提供了一个特征明确的模型系统，尤其是对疱疹病毒和腺病毒而言。丰富的遗传学、结构学和生物化学研究工作为组装模型的发展和 DNA 包装过程的理解提供了支持。在噬菌体和疱疹病毒组装的各个方面，门控复合物都是一个重要的参与者。尽管门控结构的序列相似性较低，但噬菌体中的门控结构共享门控折叠并保持保守的功能。由于其动态作用，门控蛋白具有惊人的可变性，其构象在组装的每个阶段都发生变化。由于成熟过程依赖于门控蛋白，研究人员一直在努力验证该蛋白作为一种潜在的抗病毒药物靶点的可能性。本文综述了近年来关于门控复合物在衣壳组装（包括 DNA 包装）以及门控环组装和整合中的作用，以及对门控结构的分析。
