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Structural Basis for Bacteriophage P22 Assembly and Infection Initiation.

Chunyan Wang1, Huaxin Yu1, Taehyun Park2

  • 1Microbial Sciences Institute, Yale University, West Haven, CT 06516, USA; Department of Microbial Pathogenesis, Yale School of Medicine, New Haven, CT 06536, USA.

Journal of Molecular Biology
|January 21, 2026
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Summary
This summary is machine-generated.

Salmonella phage P22

Keywords:
C12–C5 symmetry mismatch resolutionDNA translocationchannelViral infectionVirus structure

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Area of Science:

  • Bacteriophage biology
  • Structural biology
  • Microbial pathogenesis

Background:

  • Salmonella phage P22 is a model system for studying viral infection mechanisms.
  • Understanding phage-host interactions is crucial for developing phage-based therapies.
  • The tail machine of P22 is essential for host recognition and DNA injection.

Purpose of the Study:

  • To elucidate the structural basis of Salmonella phage P22 tail machine assembly and function.
  • To define the interface between the phage capsid and the tail apparatus.
  • To investigate the role of internal E proteins and the gp10 hub in assembly and infection.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine high-resolution structures.
  • Cryo-electron tomography (cryo-ET) to visualize in situ structures.
  • Biochemical analysis of protein interactions and assembly intermediates.

Main Results:

  • Detailed cryo-EM structure of wild-type P22, revealing tail apparatus assembly and portal-capsid interface.
  • Identification of flexible loop residues accommodating symmetry mismatch at the portal-capsid interface.
  • Demonstration that internal E proteins stabilize the portal protein gp1 barrel.
  • Elucidation of the gp10 hub's role in orchestrating assembly of four particle isomers.
  • Cryo-ET reveals gp10 hub as foundation for extracellular and trans-envelope channels formed by E proteins.

Conclusions:

  • The P22 tail machine exhibits intricate structural organization and dynamic flexibility.
  • Internal E proteins are critical for stabilizing the portal structure.
  • The gp10 hub is a master organizer of phage assembly and channel formation.
  • P22 employs a sophisticated mechanism for breaching the host cell envelope for genome delivery.