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

Seymour, Lisa M. and Deutscher, Ania T. and Jenkins, Cheryl and Kuit, Tracey A. and Falconer, Linda and Minion, F. Chris and Crossett, Ben and Padula, Matthew and Dixon, Nicholas E. and Djordjevic, Steven P. and Walker, Mark J. (2010) A processed multidomain hyopneumoniae adhesin binds fibronectin, plasminogen and swine respiratory cilia. Journal of Biological Chemistry, 285 (44). pp. 33971-33978. ISSN 0021-9258

Abstract

Porcine enzootic pneumonia is a chronic respiratory disease which affects swine. The aetiological agent of the disease, Mycoplasma hyopneumoniae, is a bacterium which 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 kDa 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.


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Item Type: Article (Commonwealth Reporting Category C)
Refereed: Yes
Item Status: Live Archive
Additional Information: © 2010 by The American Society for Biochemistry and Molecular Biology, Inc. Permanent restricted access to published version in accordance with the copyright policy of the publisher.
Faculty / Department / School: Historic - Faculty of Sciences - Department of Nursing
Date Deposited: 25 Jul 2014 02:27
Last Modified: 04 Mar 2015 03:52
Uncontrolled Keywords: adhesin; bacterial pathogens; bacterial species; binding proteins; C-terminal domains; cell lines; dose-dependent; epithelial cells; etiological agent; extracellular matrix components; extracellular matrix degradation; full-length proteins; multi domains; Mycoplasma hyopneumoniae; porcine kidney; proteomic analysis; respiratory disease; respiratory tract; virulence factors
Fields of Research : 07 Agricultural and Veterinary Sciences > 0707 Veterinary Sciences > 070707 Veterinary Microbiology (excl. Virology)
07 Agricultural and Veterinary Sciences > 0707 Veterinary Sciences > 070702 Veterinary Anatomy and Physiology
06 Biological Sciences > 0606 Physiology > 060602 Animal Physiology - Cell
Socio-Economic Objective: E Expanding Knowledge > 97 Expanding Knowledge > 970107 Expanding Knowledge in the Agricultural and Veterinary Sciences
Identification Number or DOI: 10.1074/jbc.M110.104463
URI: http://eprints.usq.edu.au/id/eprint/25087

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