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

Article


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 hyopneumoniae adhesin binds fibronectin, plasminogen and swine respiratory cilia." Journal of Biological Chemistry. 285 (44), pp. 33971-33978. https://doi.org/10.1074/jbc.M110.104463
Article Title

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

ERA Journal ID2230
Article CategoryArticle
AuthorsSeymour, Lisa M. (Author), Deutscher, Ania T. (Author), Jenkins, Cheryl (Author), Kuit, Tracey A. (Author), Falconer, Linda (Author), Minion, F. Chris (Author), Crossett, Ben (Author), Padula, Matthew (Author), Dixon, Nicholas E. (Author), Djordjevic, Steven P. (Author) and Walker, Mark J. (Author)
Journal TitleJournal of Biological Chemistry
Journal Citation285 (44), pp. 33971-33978
Number of Pages8
Year2010
Place of PublicationBethesda, MD. United States
ISSN0021-9258
1083-351X
Digital Object Identifier (DOI)https://doi.org/10.1074/jbc.M110.104463
Web Address (URL)http://www.jbc.org/content/285/44/33971.full.pdf+html
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.

Keywordsadhesin; 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
ANZSRC Field of Research 2020300999. Veterinary sciences not elsewhere classified
300902. Veterinary anatomy and physiology
310909. Animal physiology - cell
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Byline AffiliationsUniversity of Wollongong
Elizabeth Macarthur Agricultural Institute, Australia
Iowa State University, United States
University of Sydney
University of Technology Sydney
University of Queensland
Institution of OriginUniversity of Southern Queensland
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