Mhp 107 is a member of the multifunctional adhesin family of Mycoplasma hyopneumoniae

Publisher:
American Society for Biochemistry and Molecular Biology Inc
Publication Type:
Journal Article
Citation:
Journal Of Biological Chemistry, 2011, 286 (12), pp. 10097 - 10104
Issue Date:
2011-01
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Mycoplasma hyopneumoniae is the causative pathogen of porcine enzootic pneumonia, an economically significant disease that disrupts the mucociliary escalator in the swine respiratory tract. Expression of Mhp107, a P97 paralog encoded by the gene mhp107, was confirmed using ESI-MS/MS. To investigate the function of Mhp107, three recombinant proteins, F1Mhp107, F2Mhp107, and F3Mhp107, spanning the N-terminal, central, and C-terminal regions of Mhp107 were constructed. Colonization of swine by M. hyopneumoniae requires adherence of the bacterium to ciliated cells of the respiratory tract. Recent studies have identified a number of M. hyopneumoniae adhesins that bind heparin, fibronectin, and plasminogen. F1Mhp107 was found to bind porcine heparin (KD ~90 nm) in a dose-dependent and saturable manner, whereas F3Mhp107 bound fibronectin (KD ~180 nm) at physiologically relevant concentrations. F1Mhp107 also bound porcine plasminogen (KD = 24 nm) in a dose-dependent and physiologically relevant manner. Microspheres coated with F3Mhp107 mediate adherence to porcine kidney epithelial-like (PK15) cells, and all three recombinant proteins (F1Mhp107-F3Mhp107) bound swine respiratory cilia. Together, these findings indicate that Mhp107 is a member of the multifunctional M. hyopneumoniae adhesin family of surface proteins and contributes to both adherence to the host and pathogenesis.
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