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

Seymour, Lisa M. and Jenkins, Cheryl and Deutscher, Ania T. and Raymond, Benjamin B. A. and Padula, Matthew P. and Tacchi, Jessica L. and Bogema, Daniel R. and Eamens, Graeme J. and Woolley, Lauren K. and Dixon, Nicholas E. and 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. ISSN 1462-5814

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.


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Item Type: Article (Commonwealth Reporting Category C)
Refereed: Yes
Item Status: Live Archive
Additional Information: © 2011 Blackwell Publishing Ltd. 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 02:10
Last Modified: 02 Feb 2017 01:46
Uncontrolled Keywords: bacterial protein; fibronectin; p102 protein; plasmin; plasminogen; protein p42; protein p60; recombinant protein; tissue plasminogen activator; bacterial virulence; cell adhesion
Fields of Research : 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
Identification Number or DOI: 10.1111/j.1462-5822.2011.01702.x
URI: http://eprints.usq.edu.au/id/eprint/25088

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