Structural mechanism of bacteriophage lambda tail's interaction with the bacterial receptor.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
17 May 2024
17 May 2024
Historique:
received:
10
12
2023
accepted:
07
05
2024
medline:
18
5
2024
pubmed:
18
5
2024
entrez:
17
5
2024
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 38760367
doi: 10.1038/s41467-024-48686-3
pii: 10.1038/s41467-024-48686-3
doi:
Substances chimiques
maltoporins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
4185Subventions
Organisme : National Natural Science Foundation of China (National Science Foundation of China)
ID : 32371254
Organisme : National Natural Science Foundation of China (National Science Foundation of China)
ID : 32171190
Informations de copyright
© 2024. The Author(s).
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