Structural dynamics of bacteriophage P22 infection initiation revealed by cryo-electron tomography

Nat Microbiol. 2019 Jun;4(6):1049-1056. doi: 10.1038/s41564-019-0403-z. Epub 2019 Mar 18.

Abstract

For successful infection, bacteriophages must overcome multiple barriers to transport their genome and proteins across the bacterial cell envelope. We use cryo-electron tomography to study the infection initiation of phage P22 in Salmonella enterica serovar Typhimurium, revealing how a channel forms to allow genome translocation into the cytoplasm. Our results show free phages that initially attach obliquely to the cell through interactions between the O antigen and two of the six tailspikes; the tail needle also abuts the cell surface. The virion then orients perpendicularly and the needle penetrates the outer membrane. The needle is released and the internal head protein gp7* is ejected and assembles into an extracellular channel that extends from the gp10 baseplate to the cell surface. A second protein, gp20, is ejected and assembles into a structure that extends the extracellular channel across the outer membrane into the periplasm. Insertion of the third ejected protein, gp16, into the cytoplasmic membrane probably completes the overall trans-envelope channel into the cytoplasm. Construction of a trans-envelope channel is an essential step during infection of Gram-negative bacteria by all short-tailed phages, because such virions cannot directly deliver their genome into the cell cytoplasm.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacteriophage P22 / pathogenicity
  • Bacteriophage P22 / physiology*
  • Bacteriophage P22 / ultrastructure
  • Cell Membrane / metabolism*
  • Cell Membrane / ultrastructure
  • Cell Membrane / virology*
  • Cytoplasm / metabolism
  • Cytoplasm / virology
  • DNA, Viral
  • Electron Microscope Tomography / methods*
  • Models, Molecular
  • O Antigens
  • Protein Conformation
  • Salmonella typhimurium / virology*
  • Viral Tail Proteins / chemistry
  • Virion / metabolism
  • Virus Attachment*
  • Virus Internalization*

Substances

  • DNA, Viral
  • O Antigens
  • Viral Tail Proteins