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The structural peptidoglycan hydrolase gp181 of bacteriophage phiKZ

Yves Briers1, Konstantin Miroshnikov, Oleg Chertkov

  • 1Division of Gene Technology, Department of Biosystems, Katholieke Universiteit Leuven, Kasteelpark Arenberg 21, B-3001 Leuven, Belgium.

Biochemical and Biophysical Research Communications
|August 2, 2008
PubMed

Insights

Pseudomonas aeruginosa bacteriophage phiKZ gp181 protein contains a novel peptidoglycan hydrolase domain. This enzyme shows high activity and stability, suggesting potential for enzybiotic applications against Gram-negative bacteria.

Area of Science:

  • Microbiology
  • Virology
  • Biochemistry

Background:

  • Pseudomonas aeruginosa bacteriophage phiKZ (Myoviridae) structural protein gp181 possesses a C-terminal peptidoglycan hydrolase domain.
  • This domain is hypothesized to degrade peptidoglycan during phage infection.

Purpose of the Study:

  • To delineate and characterize the peptidoglycan hydrolase domain of gp181.
  • To evaluate its biochemical properties and potential for enzybiotic applications.

Main Methods:

  • Deletional mutagenesis to identify the active domain (gp181M8, amino acids 1880-2042).
  • Biochemical assays to assess enzyme activity, stability, and substrate specificity.
  • Comparison with phiKZ endolysin and hen egg white lysozyme.

Main Results:

  • The peptidoglycan hydrolase domain (gp181M8) was successfully delineated.
  • gp181M8 demonstrated stability at high ionic strength and thermal stress.
  • The enzyme lysed all tested outer membrane-permeabilized Gram-negative species.
  • The C-terminal region (amino acids 2043-2237) enhanced specific activity threefold.

Conclusions:

  • The novel peptidoglycan hydrolase domain of gp181 exhibits robust biochemical properties.
  • Its enhanced activity and stability make it a promising candidate for enzybiotic therapies against Gram-negative pathogens.

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