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Structure-based modification of a Clostridium difficile-targeting endolysin affects activity and host range.

Melinda J Mayer1, Vasiliki Garefalaki, Rebecca Spoerl

  • 1Institute of Food Research, Colney, Norwich NR4 7UA, United Kingdom. Melinda.Mayer@BBSRC.ac.uk

Journal of Bacteriology
|August 2, 2011
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Summary
This summary is machine-generated.

Endolysin CD27L

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Area of Science:

  • Biochemistry
  • Microbiology
  • Structural Biology

Background:

  • Clostridium difficile is a major cause of nosocomial infections.
  • Endolysins are bacteriophage-derived enzymes with antimicrobial properties.
  • CD27L is an endolysin with lytic activity against C. difficile.

Purpose of the Study:

  • To perform structural and functional analysis of CD27L's catalytic activity.
  • To investigate the role of CD27L's N-terminal domain in bacterial lysis.
  • To explore the potential for engineering endolysin specificity.

Main Methods:

  • Truncation of CD27L to its N-terminal domain (CD27L1-179).
  • Assays for lytic activity against various bacterial strains.
  • Green fluorescent protein (GFP) labeling to assess cell wall binding.
  • Crystal structure determination of CD27L1-179.
  • Structure-based sequence analysis and site-directed mutagenesis.

Main Results:

  • The N-terminal domain (CD27L1-179) showed increased lytic activity against C. difficile and other bacteria compared to full-length CD27L.
  • CD27L1-179 retained specificity, not lysing a broad range of bacteria.
  • Crystal structure revealed CD27L1-179 as a zinc-dependent N-acetylmuramoyl-l-alanine amidase.
  • Identification of key catalytic residues and substrate binding pocket.
  • Mutation of Leu 98 to Trp enhanced activity against Listeria monocytogenes.

Conclusions:

  • The N-terminal domain of CD27L possesses potent lytic activity and inherent specificity.
  • The catalytic domain alone contains features responsible for targeting specific bacterial species.
  • Endolysin specificity can be engineered through targeted mutations, offering therapeutic potential.