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Related Experiment Videos

Binding of Pseudomonas cepacia to normal human intestinal mucin and respiratory mucin from patients with cystic

U S Sajjan1, M Corey, M A Karmali

  • 1Research Institute, Hospital for Sick Children, University of Toronto, Ontario, Canada.

The Journal of Clinical Investigation
|February 1, 1992
PubMed
Summary
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Pseudomonas cepacia binds to mucins, which may be an early step in the cepacia syndrome. This binding was observed in isolates from cystic fibrosis patients, particularly those who later died from the syndrome.

Area of Science:

  • Microbiology
  • Pathogenesis
  • Biochemistry

Background:

  • Pseudomonas cepacia is an opportunistic pathogen that colonizes the lungs of cystic fibrosis patients.
  • A subset of these patients develops the severe
  • cepacia syndrome
  • leading to rapid clinical deterioration and death.

Purpose of the Study:

  • To investigate potential early bacterial attachment sites for Pseudomonas cepacia.
  • To determine if P. cepacia isolates bind to mucins from cystic fibrosis (CF) and non-CF individuals.

Main Methods:

  • Microtiter binding assays were used to measure the specific binding of P. cepacia isolates to purified CF and non-CF mucins.
  • Binding characteristics were analyzed, including saturation, inhibition by specific molecules, and effects of mucin treatments (reduction/alkylation, extraction, deglycosylation).

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  • Binding to buccal epithelial cells was also assessed.

    • Main Results:

    • 19 out of 22 P. cepacia clinical isolates bound to both CF and non-CF mucins.
    • Highest binding was observed in isolates from patients who later died with the cepacia syndrome.
    • Deglycosylation identified N-acetylglucosamine and N-acetylgalactosamine as likely mucin receptors for P. cepacia.

    Conclusions:

    • Specific binding of P. cepacia to secreted mucins is demonstrated.
    • This mucin-binding may represent an early event in the pathogenesis of the cepacia syndrome.
    • N-acetylglucosamine and N-acetylgalactosamine are implicated as key components of mucin binding sites.