Mhp107 is a member of the multifunctional adhesin family of Mycoplasma hyopneumoniae

Seymour, Lisa M. and Falconer, Linda and Deutscher, Ania T. and Minion, F. Chris and Padula, Matthew P. and Dixon, Nicholas E. and Djordjevic, Steven P. and Walker, Mark J. (2011) Mhp107 is a member of the multifunctional adhesin family of Mycoplasma hyopneumoniae. Journal of Biological Chemistry, 286 (12). pp. 10097-10104. ISSN 0021-9258

Abstract

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 adherenceof 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 (KD24~n 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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Item Type: Article (Commonwealth Reporting Category C)
Refereed: Yes
Item Status: Live Archive
Additional Information: © 2011 by The American Society for Biochemistry and Molecular Biology, Inc. Permanent restricted access to published version due to publisher copyright policy.
Faculty / Department / School: Historic - Faculty of Sciences - Department of Nursing
Date Deposited: 23 Aug 2014 20:52
Last Modified: 30 Jan 2017 06:03
Uncontrolled Keywords: adhesin; fibronectin; heparin; plasminogen; protein Mhp107; recombinant protein; ciliated cells; amino terminal sequence; animal cell; animal experiment; bacterial colonization; bacterium adherence; carboxy terminal sequence; ciliated epithelium; fibronectins
Fields of Research : 07 Agricultural and Veterinary Sciences > 0702 Animal Production > 070205 Animal Protection (Pests and Pathogens)
06 Biological Sciences > 0605 Microbiology > 060501 Bacteriology
07 Agricultural and Veterinary Sciences > 0707 Veterinary Sciences > 070707 Veterinary Microbiology (excl. Virology)
Socio-Economic Objective: E Expanding Knowledge > 97 Expanding Knowledge > 970107 Expanding Knowledge in the Agricultural and Veterinary Sciences
Funding Details:
Identification Number or DOI: 10.1074/jbc.M110.208140
URI: http://eprints.usq.edu.au/id/eprint/25089

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