Bacteriophage tail attachment protein FII / : / Phage Head-Tail Attachment / Head-to-tail joining protein W / Head-to-tail joining protein W superfamily / gpW / Minor tail protein U-like / GpU-like superfamily / Phage minor tail protein U / Phage tail protein-like superfamily ...Bacteriophage tail attachment protein FII / : / Phage Head-Tail Attachment / Head-to-tail joining protein W / Head-to-tail joining protein W superfamily / gpW / Minor tail protein U-like / GpU-like superfamily / Phage minor tail protein U / Phage tail protein-like superfamily / Phage portal protein, lambda family / Phage portal protein, lambda family 類似検索 - ドメイン・相同性
Portal protein B / Head-tail connector protein FII / Tail tube terminator protein / Head completion protein 類似検索 - 構成要素
National Natural Science Foundation of China (NSFC)
32371254
中国
National Natural Science Foundation of China (NSFC)
32171190
中国
引用
ジャーナル: J Virol / 年: 2024 タイトル: Structural morphing in the viral portal vertex of bacteriophage lambda. 著者: Zhiwei Gu / Kexun Wu / Jiawei Wang / 要旨: The portal protein of tailed bacteriophage plays essential roles in various aspects of capsid assembly, motor assembly, genome packaging, connector formation, and infection processes. After DNA ...The portal protein of tailed bacteriophage plays essential roles in various aspects of capsid assembly, motor assembly, genome packaging, connector formation, and infection processes. After DNA packaging is complete, additional proteins are assembled onto the portal to form the connector complex, which is crucial as it bridges the mature head and tail. In this study, we report high-resolution cryo-electron microscopy (cryo-EM) structures of the portal vertex from bacteriophage lambda in both its prohead and mature virion states. Comparison of these structures shows that during head maturation, in addition to capsid expansion, the portal protein undergoes conformational changes to establish interactions with the connector proteins. Additionally, the independently assembled tail undergoes morphological alterations at its proximal end, facilitating its connection to the head-tail joining protein and resulting in the formation of a stable portal-connector-tail complex. The B-DNA molecule spirally glides through the tube, interacting with the nozzle blade region of the middle-ring connector protein. These insights elucidate a mechanism for portal maturation and DNA translocation within the phage lambda system. IMPORTANCE: The tailed bacteriophages possess a distinct portal vertex that consists of a ring of 12 portal proteins associated with a 5-fold capsid shell. This portal protein is crucial in multiple ...IMPORTANCE: The tailed bacteriophages possess a distinct portal vertex that consists of a ring of 12 portal proteins associated with a 5-fold capsid shell. This portal protein is crucial in multiple stages of virus assembly and infection. Our research focused on examining the structures of the portal vertex in both its preliminary prohead state and the fully mature virion state of bacteriophage lambda. By analyzing these structures, we were able to understand how the portal protein undergoes conformational changes during maturation, the mechanism by which it prevents DNA from escaping, and the process of DNA spirally gliding.