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Molecular characterization of L-413C, a P2-related plague diagnostic bacteriophage

Emilio Garcia1, Patrick Chain, Jeff M Elliott

  • 1Chemistry, Materials and Life Sciences Directorates Lawrence Livermore National Laboratory, Livermore, CA 94550, USA. garcia12@llnl.gov

Virology
|November 30, 2007
PubMed

Insights

The plague diagnostic phage L-413C shares similarities with enterobacteriophage P2 but has a unique tail fiber protein. This mosaic protein likely explains L-413C's specific targeting of Yersinia pestis bacteria.

Area of Science:

  • Microbiology
  • Genomics
  • Molecular Biology

Background:

  • Bacteriophages are viruses that infect bacteria and are increasingly explored for therapeutic applications.
  • Phage L-413C is a diagnostic tool for plague, caused by Yersinia pestis.
  • Understanding phage-host specificity is crucial for developing targeted antimicrobial strategies.

Purpose of the Study:

  • To analyze the genome sequence and structure of the plague diagnostic phage L-413C.
  • To investigate the molecular basis for L-413C's specific recognition of Yersinia pestis.

Main Methods:

  • Whole-genome sequencing and comparative genomic analysis of phage L-413C.
  • Structural analysis of the L-413C tail fiber protein H.
  • Preadsorption experiments to assess phage binding specificity.

Main Results:

  • Phage L-413C genome is highly similar and collinear to enterobacteriophage P2.
  • L-413C possesses a mosaic tail fiber protein H, with N-terminal and C-terminal regions homologous to P2, and a central region similar to T4-related phages.
  • Preadsorption experiments confirmed that the unique H protein of L-413C is responsible for its specific binding to Yersinia pestis.

Conclusions:

  • The mosaic structure of the tail fiber protein H in L-413C is a key determinant of its specificity for Yersinia pestis.
  • The identified Yersinia pestis receptors are either absent or structurally different in Yersinia pseudotuberculosis, explaining the phage's differential targeting.

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