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

Seymour, Lisa M., Deutscher, Ania T., Jenkins, Cheryl, Kuit, Tracey A., Falconer, Linda, Minion, F. Chris, Crossett, Ben, Padula, Matthew, Dixon, Nicholas E., Djordjevic, Steven P. and Walker, Mark J. (2010) A processed Multidomain Mycoplasma hyopneumoniae adhesin binds fibronectin, plasminogen, and swine respiratory cilia. Journal of Biological Chemistry, 285 44: 33971-33978.


Author Seymour, Lisa M.
Deutscher, Ania T.
Jenkins, Cheryl
Kuit, Tracey A.
Falconer, Linda
Minion, F. Chris
Crossett, Ben
Padula, Matthew
Dixon, Nicholas E.
Djordjevic, Steven P.
Walker, Mark J.
Title A processed Multidomain Mycoplasma hyopneumoniae adhesin binds fibronectin, plasminogen, and swine respiratory cilia
Formatted title A processed Multidomain Mycoplasma hyopneumoniae adhesin binds fibronectin, plasminogen, and swine respiratory cilia
Journal name Journal of Biological Chemistry  (ERA 2012 Listed)    (ERA 2010 Rank A*)   Check publisher's open access policy
Publication date 2010-10-29
Sub-type Article
DOI 10.1074/jbc.M110.104463
Volume number 285
Issue number 44
ISSN 0021-9258; 1083-351X
Start page 33971
End page 33978
Total pages 8
Place of publication Bethesda, United States
Publisher American Society for Biochemistry and Molecular Biology
Collection year 2011
Language eng
Formatted 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 (KD 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 (KD 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. © 2010 by The American Society for Biochemistry and Molecular Biology, Inc.
Keyword Streptococcal M-protein
Elongation-factor tu
Alpha-elonase
SPF piglets
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article
Collections: Official 2011 Collection
ERA 2012 Admin Only
School of Chemistry and Molecular Biosciences
 
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Created: Sun, 07 Nov 2010, 00:08:14 EST