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Mycoplasma hyopneumoniae p65 surface lipoprotein is a lipolytic enzyme with a preference for shorter-chain fatty

Jono A Schmidt1, Glenn F Browning, Philip F Markham

  • 1Department of Veterinary Science, Veterinary Preclinical Centre, The University of Melbourne, Parkville, Victoria 3010, Australia.

Journal of Bacteriology
|August 20, 2004
PubMed

Insights

This study demonstrates that Mycoplasma hyopneumoniae p65 protein exhibits lipolytic enzyme activity. This finding is significant for understanding swine respiratory disease and mycoplasma pathogenesis.

Area of Science:

  • Microbiology
  • Veterinary Science
  • Biochemistry

Background:

  • Mycoplasma hyopneumoniae is a major bacterial pathogen causing respiratory disease in swine.
  • The p65 surface lipoprotein of M. hyopneumoniae is immunodominant and recognized during infection.
  • Sequence analysis suggested p65 belongs to the GDSL family of lipolytic enzymes.

Purpose of the Study:

  • To investigate the lipolytic activity of the M. hyopneumoniae p65 protein.
  • To characterize the enzymatic properties of recombinant p65.
  • To explore the potential role of p65 lipolytic activity in swine respiratory disease.

Main Methods:

  • Cloned and expressed the M. hyopneumoniae p65 gene in Escherichia coli.
  • Purified recombinant glutathione S-transferase (GST)-p65 fusion protein.
  • Assayed esterase and lipase activity using tributyrin agar, p-nitrophenyl esters (pNPC, pNPP), and a synthetic triglyceride.

Main Results:

  • Recombinant GST-p65 exhibited significant esterase activity against pNPC and pNPP, and lipase activity against a synthetic triglyceride.
  • Optimal activity occurred at alkaline pH (9.2-10.2) and temperatures above 39°C; calcium ions had no effect.
  • Anti-p65 antibodies inhibited both recombinant p65 activity and M. hyopneumoniae growth in vitro.

Conclusions:

  • This is the first report confirming lipolytic activity of a lipid-modified surface immunogen from Mycoplasma.
  • p65's lipolytic function may be crucial for mycoplasma nutrition and contribute to lung surfactant dysfunction in respiratory diseases.
  • Targeting p65 activity could be a strategy for controlling M. hyopneumoniae infections.

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