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Related Experiment Videos

Phosphonate catabolism by Campylobacter spp.

George L Mendz1, Francis Mégraud, Victoria Korolik

  • 1School of Biotechnology and Biomolecular Sciences, The University of New South Wales, Sydney, NSW, 2052, Australia. G.Mendz@unsw.edu.au

Archives of Microbiology
|January 14, 2005
PubMed
Summary

Campylobacter bacteria can break down phosphonates (Phn), a process typically used for survival in low-phosphate environments. These enzymes are active even when phosphate is abundant, suggesting additional roles.

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Area of Science:

  • Microbiology
  • Biochemistry
  • Molecular Biology

Background:

  • Phosphonate (Phn) compounds are crucial in various biological processes.
  • The catabolism of phosphonates is essential for nutrient acquisition in many microorganisms.
  • Campylobacter species are significant human pathogens, but their metabolic capabilities are not fully understood.

Purpose of the Study:

  • To investigate the phosphonate catabolism pathways in Campylobacter species.
  • To characterize the enzymes involved in carbon-phosphate (C-P) bond cleavage.
  • To understand the physiological role and regulation of phosphonate utilization in Campylobacter.

Main Methods:

  • Nuclear magnetic resonance (NMR) spectroscopy.
  • Bacterial cell culture and whole-cell lysate preparation.

Related Experiment Videos

  • Enzyme kinetics assays and substrate competition experiments.
  • In silico genomic analysis of Campylobacter jejuni.

    • Main Results:

    • Campylobacter spp. demonstrated the ability to cleave phosphonate bonds in various compounds.
    • Enzyme activities were localized to cell-wall and cytosolic fractions.
    • At least two distinct enzymatic activities were implicated in C-P bond cleavage.
    • Unlike other bacteria, phosphonate catabolism in Campylobacter was expressed in phosphate-rich media and induced growth in phosphate-deficient conditions.
    • No known orthologous genes for C-P bond-cleaving enzymes were found in the Campylobacter jejuni genome.

    Conclusions:

    • Campylobacter possesses novel mechanisms for phosphonate utilization, potentially serving as a survival strategy in phosphate-limited environments.
    • The constitutive expression of these enzymes suggests additional physiological functions beyond phosphate scavenging.
    • Further research is needed to identify the specific enzymes and their roles in Campylobacter physiology.