PDF(Pubmed)
Abstract：
Infection of bacteria by phages is a complex multi-step process that includes specific recognition of the host cell, creation of a temporary breach in the host envelope, and ejection of viral DNA into the bacterial cytoplasm. These steps must be perfectly regulated to ensure efficient infection. Here we report the dual function of the tail completion protein gp16.1 of bacteriophage SPP1. First, gp16.1 has an auxiliary role in assembly of the tail interface that binds to the capsid connector. Second, gp16.1 is necessary to ensure correct routing of phage DNA to the bacterial cytoplasm. Viral particles assembled without gp16.1 are indistinguishable from wild-type virions and eject DNA normally in vitro. However, they release their DNA to the extracellular space upon interaction with the host bacterium. The study shows that a highly conserved tail completion protein has distinct functions at two essential steps of the virus life cycle in long-tailed phages.
摘要：
噬菌体感染细菌是一个复杂的多步骤过程，包括对宿主细胞的特异性识别，在主机信封中创建临时缺口，并将病毒DNA注入细菌细胞质。必须对这些步骤进行完美调节，以确保有效的感染。在这里，我们报告了噬菌体SPP1的尾部完成蛋白gp16.1的双重功能。首先,gp16.1在绑定到衣壳连接器的尾部接口的组装中具有辅助作用。第二,gp16.1是确保噬菌体DNA正确路由到细菌细胞质所必需的。在没有gp16.1的情况下组装的病毒颗粒与野生型病毒颗粒无法区分,并且通常在体外排出DNA。然而,它们在与宿主细菌相互作用后将DNA释放到细胞外空间。研究表明，在长尾噬菌体中，高度保守的尾部完成蛋白在病毒生命周期的两个基本步骤中具有不同的功能。
