Mhp182 (P102) binds fibronectin and contributes to the recruitment of plasmin(ogen) to the Mycoplasma hyopneumoniae cell surface

Article


Seymour, Lisa M., Jenkins, Cheryl, Deutscher, Ania T., Raymond, Benjamin B. A., Padula, Matthew P., Tacchi, Jessica L., Bogema, Daniel R., Eamens, Graeme J., Woolley, Lauren K., Dixon, Nicholas E., Walker, Mark J. and Djordjevic, Steven P.. 2012. "Mhp182 (P102) binds fibronectin and contributes to the recruitment of plasmin(ogen) to the Mycoplasma hyopneumoniae cell surface." Cellular Microbiology. 14 (1), pp. 81-94. https://doi.org/10.1111/j.1462-5822.2011.01702.x
Article Title

Mhp182 (P102) binds fibronectin and contributes to the recruitment of plasmin(ogen) to the Mycoplasma hyopneumoniae cell surface

ERA Journal ID2526
Article CategoryArticle
AuthorsSeymour, Lisa M. (Author), Jenkins, Cheryl (Author), Deutscher, Ania T. (Author), Raymond, Benjamin B. A. (Author), Padula, Matthew P. (Author), Tacchi, Jessica L. (Author), Bogema, Daniel R. (Author), Eamens, Graeme J. (Author), Woolley, Lauren K. (Author), Dixon, Nicholas E. (Author), Walker, Mark J. (Author) and Djordjevic, Steven P. (Author)
Journal TitleCellular Microbiology
Journal Citation14 (1), pp. 81-94
Number of Pages14
Year2012
Place of PublicationChichester, West Sussex. United Kingdom
ISSN1462-5814
1462-5822
Digital Object Identifier (DOI)https://doi.org/10.1111/j.1462-5822.2011.01702.x
Abstract

Mycoplasma hyopneumoniae is a major, economically damaging respiratory pathogen. Although M. hyopneumoniae cells bind plasminogen, the identification of plasminogen-binding surface proteins and the biological ramifications of acquiring plasminogen requires further investigation.
mhp182 encodes a highly expressed 102 kDa protein (P102) that undergoes proteolytic processing to generate surface-located N-terminal 60 kDa
(P60) and C-terminal 42 kDa (P42) proteins of unknown function. We show that recombinant P102 (rP102) binds plasminogen at physiologically relevant concentrations (KD ~ 76 nM) increasing the susceptibility of plasmin(ogen) to activation by tissue-specific plasminogen activator (tPA).
Recombinant proteins constructed to mimic P60 (rP60) and P42 (rP42) also bound plasminogen at physiologically significant levels. M. hyopneumoniae
surface-bound plasminogen was activated by tPA and is able to degrade fibrinogen, demonstrating the biological functionality of M. hyopneumoniae-bound plasmin(ogen) upon activation. Plasmin(ogen) was readily detected in porcine ciliated airways and plasmin levels were consistently higher in bronchoalveolar lavage fluid from M. hyopneumoniae-infected animals. Additionally, rP102 and rP42 bind fibronectin with KDs of 26 and 33 nM respectively and recombinant P102 proteins promote adherence to porcine kidney epithelial-like cells. The multifunctional binding ability of P102 and activation of M. hyopneumoniae-sequestered plasmin(ogen) by an exogenous activator suggests P102 plays an important role in virulence.

Keywordsbacterial protein; fibronectin; p102 protein; plasmin; plasminogen; protein p42; protein p60; recombinant protein; tissue plasminogen activator; bacterial virulence; cell adhesion
ANZSRC Field of Research 2020300999. Veterinary sciences not elsewhere classified
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Byline AffiliationsUniversity of Wollongong
Elizabeth Macarthur Agricultural Institute, Australia
University of Technology Sydney
Department of Primary Industries, New South Wales
University of Queensland
Institution of OriginUniversity of Southern Queensland
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