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The tape measure protein of the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA35 has an active muramidase domain

Lorena Rodríguez-Rubio1, Dolores Gutiérrez, Beatriz Martínez

  • 1Instituto de Productos Lácteos de Asturias (IPLA-CSIC), Department of Technology and Biotechnology of Dairy Products, Asturias, Spain.

Applied and Environmental Microbiology
|June 26, 2012
PubMed

Insights

Staphylococcus aureus bacteriophage vB_SauS-phiIPLA35's tape measure protein contains a lysozyme-like domain (TG1) with muramidase activity. This domain shows in vitro lytic activity against live Staphylococcus aureus cells, offering potential for infection treatment.

Area of Science:

  • Microbiology
  • Virology
  • Biochemistry

Background:

  • Tailed double-stranded DNA (dsDNA) bacteriophages often possess structural proteins with peptidoglycan hydrolytic functions.
  • The tape measure protein of Staphylococcus aureus bacteriophage vB_SauS-phiIPLA35 includes both a lysozyme-like and a peptidase_M23 domain.

Purpose of the Study:

  • To investigate the enzymatic activity of the lysozyme-like domain (TG1) from Staphylococcus aureus bacteriophage vB_SauS-phiIPLA35.
  • To assess the lytic potential of the TG1 domain against live Staphylococcus aureus cells.

Main Methods:

  • Characterization of the lysozyme-like domain (TG1) of the tape measure protein.
  • In vitro assays to determine muramidase activity.
  • Testing lytic activity against live Staphylococcus aureus bacterial cells.

Main Results:

  • The lysozyme-like domain (TG1) was confirmed to possess muramidase activity.
  • TG1 demonstrated in vitro lytic activity against live Staphylococcus aureus cells.

Conclusions:

  • The lysozyme-like domain (TG1) of the Staphylococcus aureus tape measure protein exhibits enzymatic activity.
  • This domain's lytic properties suggest potential applications in treating bacterial infections.

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