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

Seymour, LM; Jenkins, C; Deutscher, AT; Raymond, BBA; Padula, MP; Tacchi, JL; Bogema, DR; Eamens, GJ; Woolley, LK; Dixon, NE; Walker, MJ; Djordjevic, SP

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

Seymour, LM Jenkins, C

Deutscher, AT Raymond, BBA

Padula, MP

Tacchi, JL Bogema, DR

Eamens, GJ Woolley, LK Dixon, NE Walker, MJ Djordjevic, SP

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Publication Type:: Journal Article
Citation:: Cellular Microbiology, 2012, 14 (1), pp. 81 - 94
Issue Date:: 2012-01-01

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Field	Value	Language
dc.contributor.author	Seymour, LM	en_US
dc.contributor.author	Jenkins, C https://orcid.org/0000-0002-5966-072X	en_US
dc.contributor.author	Deutscher, AT	en_US
dc.contributor.author	Raymond, BBA https://orcid.org/0000-0003-3610-9289	en_US
dc.contributor.author	Padula, MP https://orcid.org/0000-0002-8283-0643	en_US
dc.contributor.author	Tacchi, JL	en_US
dc.contributor.author	Bogema, DR https://orcid.org/0000-0001-7013-7326	en_US
dc.contributor.author	Eamens, GJ	en_US
dc.contributor.author	Woolley, LK	en_US
dc.contributor.author	Dixon, NE	en_US
dc.contributor.author	Walker, MJ	en_US
dc.contributor.author	Djordjevic, SP https://orcid.org/0000-0001-9301-5372	en_US
dc.date.issued	2012-01-01	en_US
dc.identifier.citation	Cellular Microbiology, 2012, 14 (1), pp. 81 - 94	en_US
dc.identifier.issn	1462-5814	en_US
dc.identifier.uri	http://hdl.handle.net/10453/18179
dc.description.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 102kDa protein (P102) that undergoes proteolytic processing to generate surface-located N-terminal 60kDa (P60) and C-terminal 42kDa (P42) proteins of unknown function. We show that recombinant P102 (rP102) binds plasminogen at physiologically relevant concentrations (K D~76nM) 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 K Ds of 26 and 33nM 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. © 2011 Blackwell Publishing Ltd.	en_US
dc.relation.ispartof	Cellular Microbiology	en_US
dc.relation.isbasedon	10.1111/j.1462-5822.2011.01702.x	en_US
dc.subject.classification	Microbiology	en_US
dc.subject.mesh	Cells, Cultured	en_US
dc.subject.mesh	Epithelial Cells	en_US
dc.subject.mesh	Animals	en_US
dc.subject.mesh	Swine	en_US
dc.subject.mesh	Mycoplasma hyopneumoniae	en_US
dc.subject.mesh	Pneumonia of Swine, Mycoplasmal	en_US
dc.subject.mesh	Plasminogen	en_US
dc.subject.mesh	Adhesins, Bacterial	en_US
dc.subject.mesh	Fibronectins	en_US
dc.subject.mesh	Recombinant Proteins	en_US
dc.subject.mesh	Bacterial Adhesion	en_US
dc.subject.mesh	Amino Acid Sequence	en_US
dc.subject.mesh	Protein Binding	en_US
dc.subject.mesh	Molecular Sequence Data	en_US
dc.subject.mesh	Fibrinolysin	en_US
dc.title	Mhp182 (P102) binds fibronectin and contributes to the recruitment of plasmin(ogen) to the Mycoplasma hyopneumoniae cell surface	en_US
dc.type	Journal Article
utslib.citation.volume	1	en_US
utslib.citation.volume	14	en_US
utslib.for	0605 Microbiology	en_US
utslib.for	1108 Medical Microbiology	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
pubs.organisational-group	/University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation
utslib.copyright.status	closed_access
pubs.issue	1	en_US
pubs.publication-status	Published	en_US
pubs.volume	14	en_US

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 102kDa protein (P102) that undergoes proteolytic processing to generate surface-located N-terminal 60kDa (P60) and C-terminal 42kDa (P42) proteins of unknown function. We show that recombinant P102 (rP102) binds plasminogen at physiologically relevant concentrations (K D~76nM) 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 K Ds of 26 and 33nM 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. © 2011 Blackwell Publishing Ltd.

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http://hdl.handle.net/10453/18179