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Proteolytic processing of the cilium adhesin MHJ_0194 (P123J ) in Mycoplasma hyopneumoniae generates a functionally

Benjamin B A Raymond1, Cheryl Jenkins, Lisa M Seymour

  • 1The ithree Institute, University of Technology, Sydney, NSW, Australia.

Cellular Microbiology
|October 9, 2014
PubMed

Insights

Mycoplasma hyopneumoniae extensively processes its P123 adhesin, revealing new binding sites. This bacterium manipulates host fibronectin deposition, influencing host cell interactions during infection.

Area of Science:

  • Microbiology
  • Cell Biology
  • Veterinary Science

Background:

  • Mycoplasma hyopneumoniae causes significant respiratory disease in pigs.
  • The bacterium utilizes surface proteins, like P123 adhesin, for host cell attachment.
  • Previous studies indicated complex processing of P123, but detailed characterization was lacking.

Purpose of the Study:

  • To comprehensively characterize the extensive proteolytic processing of Mycoplasma hyopneumoniae's P123 adhesin.
  • To investigate the adhesive properties of P123 cleavage fragments and identify novel binding motifs.
  • To examine the in vivo interaction between M. hyopneumoniae and host fibronectin.

Main Methods:

  • Affinity chromatography using heparin, fibronectin, and plasminogen as bait.
  • Peptide array analysis to identify binding motifs.
  • Immunohistochemistry to study in vivo host-pathogen interactions.

Main Results:

  • Detailed characterization of extensive P123 processing events beyond previously known cleavages.
  • Identification of a novel binding motif within the C-terminus of P123.
  • Demonstration that M. hyopneumoniae induces fibronectin deposition at the infection site on ciliated epithelium.

Conclusions:

  • Mycoplasma hyopneumoniae possesses sophisticated molecular mechanisms for host cell adhesion and interaction.
  • The processing of P123 adhesin generates fragments with significant adhesive capabilities.
  • The bacterium actively influences host extracellular matrix deposition, suggesting modulation of host cell communication pathways.

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