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A processed multidomain Mycoplasma hyopneumoniae adhesin binds fibronectin, plasminogen, and swine respiratory cilia

Journal Article


Abstract


  • Porcine enzootic pneumonia is a chronic respiratory disease that affects swine. The etiological agent of the disease, Mycoplasma hyopneumoniae, is a bacterium that adheres to cilia of the swine respiratory tract, resulting in loss of cilia and epithelial cell damage. A M. hyopneumoniae protein P116, encoded by mhp108, was investigated as a potential adhesin. Examination of P116 expression using proteomic analyses observed P116 as a full-length protein and also as fragments, ranging from 17 to 70 kDa in size. A variety of pathogenic bacterial species have been shown to bind the extracellular matrix component fibronectin as an adherence mechanism. M. hyopneumoniae cells were found to bind fibronectin in a dose-dependent and saturable manner. Surface plasmon resonance was used to show that a recombinant C-terminal domain of P116 bound fibronectin at physiologically relevant concentrations (K-D 24 +/- 6 nM). Plasmin(ogen)-binding proteins are also expressed by many bacterial pathogens, facilitating extracellular matrix degradation. M. hyopneumoniae cells were found to also bind plasminogen in a dose-dependent and saturable manner; the C-terminal domain of P116 binds to plasminogen (K-D 44 +/- 5 nM). Plasminogen binding was abolished when the C-terminal lysine of P116 was deleted, implicating this residue as part of the plasminogen binding site. P116 fragments adhere to the PK15 porcine kidney epithelial-like cell line and swine respiratory cilia. Collectively these data suggest that P116 is an important adhesin and virulence factor of M. hyopneumoniae.

Authors


  •   Seymour, Lisa M. (external author)
  •   Deutscher, Ania T. (external author)
  •   Jenkins, Cheryl (external author)
  •   Kuit, Tracey A.
  •   Falconer, Linda (external author)
  •   Minion, F Chris (external author)
  •   Crossett, Ben (external author)
  •   Padula, Matthew P. (external author)
  •   Dixon, Nicholas E.
  •   Djordjevic, Steven P. (external author)
  •   Walker, Mark J. (external author)

Publication Date


  • 2010

Citation


  • Seymour, L., Deutscher, A., Jenkins, C., Kuit, T. A., Falconer, L., Minion, F., Crossett, B., Padula, M. P., Dixon, N. E., Djordjevic, S. & Walker, M. J. (2010). A processed multidomain Mycoplasma hyopneumoniae adhesin binds fibronectin, plasminogen, and swine respiratory cilia. Journal of Biological Chemistry, 285 (44), 33971-33978.

Scopus Eid


  • 2-s2.0-77958599627

Ro Metadata Url


  • http://ro.uow.edu.au/scipapers/5147

Has Global Citation Frequency


Number Of Pages


  • 7

Start Page


  • 33971

End Page


  • 33978

Volume


  • 285

Issue


  • 44

Abstract


  • Porcine enzootic pneumonia is a chronic respiratory disease that affects swine. The etiological agent of the disease, Mycoplasma hyopneumoniae, is a bacterium that adheres to cilia of the swine respiratory tract, resulting in loss of cilia and epithelial cell damage. A M. hyopneumoniae protein P116, encoded by mhp108, was investigated as a potential adhesin. Examination of P116 expression using proteomic analyses observed P116 as a full-length protein and also as fragments, ranging from 17 to 70 kDa in size. A variety of pathogenic bacterial species have been shown to bind the extracellular matrix component fibronectin as an adherence mechanism. M. hyopneumoniae cells were found to bind fibronectin in a dose-dependent and saturable manner. Surface plasmon resonance was used to show that a recombinant C-terminal domain of P116 bound fibronectin at physiologically relevant concentrations (K-D 24 +/- 6 nM). Plasmin(ogen)-binding proteins are also expressed by many bacterial pathogens, facilitating extracellular matrix degradation. M. hyopneumoniae cells were found to also bind plasminogen in a dose-dependent and saturable manner; the C-terminal domain of P116 binds to plasminogen (K-D 44 +/- 5 nM). Plasminogen binding was abolished when the C-terminal lysine of P116 was deleted, implicating this residue as part of the plasminogen binding site. P116 fragments adhere to the PK15 porcine kidney epithelial-like cell line and swine respiratory cilia. Collectively these data suggest that P116 is an important adhesin and virulence factor of M. hyopneumoniae.

Authors


  •   Seymour, Lisa M. (external author)
  •   Deutscher, Ania T. (external author)
  •   Jenkins, Cheryl (external author)
  •   Kuit, Tracey A.
  •   Falconer, Linda (external author)
  •   Minion, F Chris (external author)
  •   Crossett, Ben (external author)
  •   Padula, Matthew P. (external author)
  •   Dixon, Nicholas E.
  •   Djordjevic, Steven P. (external author)
  •   Walker, Mark J. (external author)

Publication Date


  • 2010

Citation


  • Seymour, L., Deutscher, A., Jenkins, C., Kuit, T. A., Falconer, L., Minion, F., Crossett, B., Padula, M. P., Dixon, N. E., Djordjevic, S. & Walker, M. J. (2010). A processed multidomain Mycoplasma hyopneumoniae adhesin binds fibronectin, plasminogen, and swine respiratory cilia. Journal of Biological Chemistry, 285 (44), 33971-33978.

Scopus Eid


  • 2-s2.0-77958599627

Ro Metadata Url


  • http://ro.uow.edu.au/scipapers/5147

Has Global Citation Frequency


Number Of Pages


  • 7

Start Page


  • 33971

End Page


  • 33978

Volume


  • 285

Issue


  • 44