maltodextrin transmembrane transporter activity / maltose transporting porin activity / symbiont genome ejection through host cell envelope, long flexible tail mechanism / viral tail assembly / virus tail / pore complex / monoatomic ion transport / cell outer membrane / host cell cytoplasm / entry receptor-mediated virion attachment to host cell ...maltodextrin transmembrane transporter activity / maltose transporting porin activity / symbiont genome ejection through host cell envelope, long flexible tail mechanism / viral tail assembly / virus tail / pore complex / monoatomic ion transport / cell outer membrane / host cell cytoplasm / entry receptor-mediated virion attachment to host cell / receptor-mediated virion attachment to host cell / virion attachment to host cell 類似検索 - 分子機能
Maltoporin / Porin, LamB-type / Porin, LamB-type superfamily / LamB porin / Domain of unknown function DUF1983 / Domain of unknown function DUF3672 / : / Domain of unknown function (DUF1983) / Fibronectin type III protein / Tip attachment protein J ...Maltoporin / Porin, LamB-type / Porin, LamB-type superfamily / LamB porin / Domain of unknown function DUF1983 / Domain of unknown function DUF3672 / : / Domain of unknown function (DUF1983) / Fibronectin type III protein / Tip attachment protein J / Putative phage tail protein / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin-like fold 類似検索 - ドメイン・相同性
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: Nat Commun / 年: 2024 タイトル: Structural mechanism of bacteriophage lambda tail's interaction with the bacterial receptor. 著者: Xiaofei Ge / Jiawei Wang / 要旨: Bacteriophage infection, a pivotal process in microbiology, initiates with the phage's tail recognizing and binding to the bacterial cell surface, which then mediates the injection of viral DNA. ...Bacteriophage infection, a pivotal process in microbiology, initiates with the phage's tail recognizing and binding to the bacterial cell surface, which then mediates the injection of viral DNA. Although comprehensive studies on the interaction between bacteriophage lambda and its outer membrane receptor, LamB, have provided rich information about the system's biochemical properties, the precise molecular mechanism remains undetermined. This study revealed the high-resolution cryo-electron microscopy (cryo-EM) structures of the bacteriophage lambda tail complexed with its irreversible Shigella sonnei 3070 LamB receptor and the closed central tail fiber. These structures reveal the complex processes that trigger infection and demonstrate a substantial conformational change in the phage lambda tail tip upon LamB binding. Providing detailed structures of bacteriophage lambda infection initiation, this study contributes to the expanding knowledge of lambda-bacterial interaction, which holds significance in the fields of microbiology and therapeutic development.