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Penicillin binding proteins of Vibrio cholerae

T K Sengupta1, A N Chatterjee, J Das

  • 1Biophysics Division, Indian Institute of Chemical Biology, Calcutta.

Biochemical and Biophysical Research Communications
|September 28, 1990
PubMed

Insights

This study identified eleven penicillin-binding proteins (PBPs) in Vibrio cholerae, revealing their inner membrane localization and varying molecular weights. Specific antibiotics like cephaloridine, aztreonam, and mecillinam show distinct binding affinities to these PBPs.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Vibrio cholerae is a significant human pathogen responsible for cholera.
  • Penicillin-binding proteins (PBPs) are crucial enzymes involved in bacterial cell wall synthesis and are primary targets for beta-lactam antibiotics.
  • Understanding the specific PBPs in V. cholerae is essential for developing targeted antibacterial therapies.

Purpose of the Study:

  • To identify and characterize the penicillin-binding proteins (PBPs) present in Vibrio cholerae.
  • To investigate the binding affinities of different beta-lactam antibiotics to these identified PBPs.

Main Methods:

  • Utilized [125I] labelled p-hydroxybenzyl penicillin (PenX) for the identification of PBPs in Vibrio cholerae.
  • Determined protein localization to the inner membrane and molecular weights.
  • Employed neutral hydroxylamine to release labelled PenX and cold benzyl penicillin for inhibition assays.
  • Assessed the binding of cephaloridine, aztreonam, and mecillinam to specific PBPs.

Main Results:

  • Eleven distinct penicillin-binding proteins (PBPs) were identified in Vibrio cholerae, located in the inner membrane with molecular weights ranging from 97,000 to 22,000.
  • PBP 4 demonstrated the highest sensitivity to both cephaloridine and aztreonam.
  • Cephaloridine also bound to high molecular weight PBPs 1, 2, and 3, while aztreonam additionally bound to PBP 7.
  • Mecillinam exhibited affinity for PBPs 1, 4, and 11.

Conclusions:

  • The study successfully identified and characterized eleven PBPs in Vibrio cholerae, providing a molecular basis for their susceptibility to various antibiotics.
  • Differential binding of cephaloridine, aztreonam, and mecillinam to specific PBPs suggests potential for developing targeted therapies against V. cholerae infections.
  • Further research into these PBP-antibiotic interactions could lead to novel strategies for combating cholera.

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