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Defects in glycopeptidolipid biosynthesis confer phage I3 resistance in Mycobacterium smegmatis

Jiemin Chen1, Jordan Kriakov2, Albel Singh1

  • 1School of Biosciences, College of Life and Environmental Sciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.

Microbiology (Reading, England)
|September 12, 2009
PubMed

Insights

Mycobacteriophage I3 uses a specific methylated rhamnose on Mycobacterium smegmatis glycopeptidolipids (GPLs) as its receptor. This finding advances understanding of phage-host interactions and mycobacterial cell wall structure.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Virology

Background:

  • Mycobacteriophages are vital tools for studying mycobacteria, including Mycobacterium tuberculosis.
  • Understanding mycobacteriophage infection mechanisms and receptors is crucial but limited.
  • Phage I3 resistance was investigated to identify its specific receptor.

Purpose of the Study:

  • To identify the specific receptor for mycobacteriophage I3.
  • To elucidate the role of glycopeptidolipids (GPLs) in phage I3 infection.
  • To define the minimal structural component of GPLs essential for phage I3 binding.

Main Methods:

  • Screening of Mycobacterium smegmatis transposon mutants for phage I3 resistance.
  • Analysis of transposon insertion sites in resistant mutants.
  • Testing phage sensitivity of previously characterized GPL-deficient mutants.
  • Defining the critical GPL structural component for phage binding.

Main Results:

  • Phage I3-resistant mutants had insertions in GPL biosynthesis genes, lacking GPLs.
  • GPL deficiency specifically conferred resistance to phage I3, not D29 or Bxz1.
  • A single methylated rhamnose residue on the GPL core was identified as critical for phage I3 binding.

Conclusions:

  • Glycopeptidolipids (GPLs) are essential for mycobacteriophage I3 infection.
  • A specific methylated rhamnose moiety on the GPL structure serves as the minimal receptor for phage I3.
  • This research clarifies phage-host interactions and provides insights into mycobacterial cell wall structure.

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