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PlyC: a multimeric bacteriophage lysin.

Daniel Nelson1, Raymond Schuch, Peter Chahales

  • 1Laboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA. nelsond@rockefeller.edu

Proceedings of the National Academy of Sciences of the United States of America
|July 5, 2006
PubMed
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Bacteriophage lysins are potent antimicrobials. This study reveals a novel two-protein lysin, PlyC, with separate catalytic (PlyCA) and binding (PlyCB) components, offering new antimicrobial strategies.

Area of Science:

  • Microbiology
  • Biochemistry
  • Structural Biology

Background:

  • Bacteriophage lysins are enzymes targeting bacterial cell walls for phage release.
  • Gram-positive lysins typically feature a single polypeptide with catalytic and cell-wall-binding domains.
  • Existing lysins represent a unique antimicrobial strategy due to rapid bacterial lysis.

Purpose of the Study:

  • To characterize a novel lysin, PlyC, from streptococcal bacteriophage C(1).
  • To elucidate the composition and function of the PlyC lysin system.
  • To define the structural family and active site of this unique enzyme.

Main Methods:

  • Cloning and expression of the plyC operon.
  • Biochemical and biophysical studies to determine holoenzyme composition.

Related Experiment Videos

  • Inhibitor studies, bioinformatic analysis, and point mutagenesis to identify active-site residues.

    • Main Results:

    • PlyC is composed of two distinct gene products: PlyCA (catalytic) and PlyCB (binding).
    • The active PlyC holoenzyme comprises eight PlyCB subunits per PlyCA subunit.
    • PlyCA contains a cysteine, histidine-dependent amidohydrolase/peptidase domain with Cys-333 and His-420 as active-site residues.
    • PlyCB self-assembles into an octamer responsible for cell-wall binding.

    Conclusions:

    • PlyC represents a previously uncharacterized structural family of cell-wall hydrolases.
    • The two-component system of PlyC (PlyCA and PlyCB) is distinct from known single-polypeptide lysins.
    • This discovery opens new avenues for developing targeted antimicrobial agents based on novel lysin structures.