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

Article


Seymour, Lisa M., Falconer, Linda, Deutscher, Ania T., Minion, F. Chris, Padula, Matthew P., Dixon, Nicholas E., 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. https://doi.org/10.1074/jbc.M110.208140
Article Title

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

ERA Journal ID2230
Article CategoryArticle
AuthorsSeymour, Lisa M. (Author), Falconer, Linda (Author), Deutscher, Ania T. (Author), Minion, F. Chris (Author), Padula, Matthew P. (Author), Dixon, Nicholas E. (Author), Djordjevic, Steven P. (Author) and Walker, Mark J. (Author)
Journal TitleJournal of Biological Chemistry
Journal Citation286 (12), pp. 10097-10104
Number of Pages8
Year2011
Place of PublicationRockville, MD. United States
ISSN0021-9258
1083-351X
Digital Object Identifier (DOI)https://doi.org/10.1074/jbc.M110.208140
Web Address (URL)http://www.jbc.org/content/286/12/10097
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.

Keywordsadhesin; 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
ANZSRC Field of Research 2020300304. Animal protection (incl. pests and pathogens)
310701. Bacteriology
300999. Veterinary sciences not elsewhere classified
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Byline AffiliationsUniversity of Wollongong
Elizabeth Macarthur Agricultural Institute, Australia
Iowa State University, United States
University of Technology Sydney
University of Queensland
Institution of OriginUniversity of Southern Queensland
Funding source
Australian Research Council (ARC)
Grant ID
LP776771
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