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Penicillin-binding proteins of listeria monocytogenes--a re-evaluation

Dorota Korsak1, Joanna J Zawadzka, Maria E Siwińska

  • 1Department of Bacterial Physiology, Institute of Microbiology, University of Warsaw, Poland,

Acta Microbiologica Polonica
|August 20, 2002
PubMed

Insights

Researchers identified penicillin-binding proteins (PBPs) in Listeria monocytogenes using radiolabeled penicillin. This method quantifies PBPs in the cytoplasmic membrane after cell wall murein disruption.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Penicillin-binding proteins (PBPs) are essential targets for beta-lactam antibiotics.
  • Understanding PBP localization and quantity is crucial for antibiotic development.
  • Listeria monocytogenes is a significant foodborne pathogen requiring effective treatment strategies.

Purpose of the Study:

  • To identify and characterize penicillin-binding proteins (PBPs) in the cytoplasmic membrane of Listeria monocytogenes.
  • To develop a method for quantifying PBP copy numbers within the bacterial cell.

Main Methods:

  • Treatment of intact Listeria monocytogenes cells and isolated membranes with [3H]penicillin.
  • Disruption of the cell wall murein using Listeria monocytogenes bacteriophage lysin.
  • Modified procedure based on Dougherty et al. (1996) for PBP molecular weight (M(r)) evaluation and quantitation.

Main Results:

  • Successfully identified PBPs located in the cytoplasmic membrane of Listeria monocytogenes.
  • Quantified the molecular weights (M(r)s) of individual PBPs.
  • Determined the copy number of each PBP within the bacterial cell.

Conclusions:

  • The study established a reliable method for identifying and quantifying PBPs in Listeria monocytogenes.
  • This methodology provides insights into PBP expression levels, potentially aiding in the development of new antibiotics targeting this pathogen.

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