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Structural Analysis of Jumbo Coliphage phAPEC6.

Jeroen Wagemans1, Jessica Tsonos1,2,3, Dominique Holtappels1

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International Journal of Molecular Sciences
|May 2, 2020
PubMed
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The Escherichia coli virus phAPEC6 has a complex structure, including a major capsid protein and unique hairy fibers. Cryo-electron microscopy revealed details of its DNA packaging and tail assembly, suggesting roles in host interaction.

Keywords:
HK97-foldcryo-EMjumbo phage

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Area of Science:

  • Bacteriophage biology
  • Structural virology
  • Microbial genomics

Background:

  • The genome of Escherichia coli virus phAPEC6 contains 551 predicted gene products.
  • A significant majority (83%) of these gene products have unknown functions.
  • 62 virion-associated proteins were identified using mass spectrometry (ESI-MS/MS).

Purpose of the Study:

  • To elucidate the structural organization of the Escherichia coli virus phAPEC6.
  • To characterize key structural components, including capsid proteins, DNA packaging, and tail structures.
  • To investigate the potential function of unique phage structures like hairy fibers.

Main Methods:

  • Mass spectrometry (ESI-MS/MS) for protein identification.
  • Cryo-electron microscopy (Cryo-EM) for high-resolution structural analysis.
  • Transmission electron microscopy (TEM) for initial structural observations.

Main Results:

  • The major capsid protein (Gp225) exhibits an HK97 fold and is present in high copy numbers (1620).
  • phAPEC6 DNA (350 kbp) is packaged in at least 15 concentric layers within the capsid.
  • A contractile tail with 25 hexameric rings (Gp277) and unique, ordered hairy fibers were visualized.

Conclusions:

  • The structural analysis provides insights into the complex assembly and packaging mechanisms of phAPEC6.
  • The identified virion-associated proteins and structural features contribute to understanding phage biology.
  • The unique hairy fibers may play a role in the interaction of phAPEC6 with its host, Escherichia coli.