The Central Spike Complex of Bacteriophage T4 Contacts PpiD in the Periplasm of Escherichia coli

Viruses. 2020 Oct 6;12(10):1135. doi: 10.3390/v12101135.


Infecting bacteriophage T4 uses a contractile tail structure to breach the envelope of the Escherichia coli host cell. During contraction, the tail tube headed with the "central spike complex" is thought to mechanically puncture the outer membrane. We show here that a purified tip fragment of the central spike complex interacts with periplasmic chaperone PpiD, which is anchored to the cytoplasmic membrane. PpiD may be involved in the penetration of the inner membrane by the T4 injection machinery, resulting in a DNA-conducting channel to translocate the phage DNA into the interior of the cell. Host cells with the ppiD gene deleted showed partial reduction in the plating efficiency of T4, suggesting a supporting role of PpiD to improve the efficiency of the infection process.

Keywords: DNA translocation; Keywords: bacteriophage T4; periplasmic chaperone; tail structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacteriophage T4 / metabolism*
  • Cell Membrane / metabolism
  • Escherichia coli / virology*
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism*
  • Glycoside Hydrolases
  • Peptidylprolyl Isomerase / genetics
  • Peptidylprolyl Isomerase / metabolism*
  • Periplasm / virology
  • Viral Envelope Proteins / metabolism
  • Viral Tail Proteins / metabolism*
  • Virus Attachment
  • Virus Internalization


  • Escherichia coli Proteins
  • Viral Envelope Proteins
  • Viral Tail Proteins
  • Glycoside Hydrolases
  • tailspike protein, bacteriophage
  • PpiD protein, E coli
  • Peptidylprolyl Isomerase