Proteolytic processing of the cilium adhesin MHJ_0194 (P123<inf>J</inf>) in Mycoplasma hyopneumoniae generates a functionally diverse array of cleavage fragments that bind multiple host molecules

Raymond, BBA; Jenkins, C; Seymour, LM; Tacchi, JL; Widjaja, M; Jarocki, VM; Deutscher, AT; Turnbull, L; Whitchurch, CB; Padula, MP; Djordjevic, SP

Proteolytic processing of the cilium adhesin MHJ_0194 (P123<inf>J</inf>) in Mycoplasma hyopneumoniae generates a functionally diverse array of cleavage fragments that bind multiple host molecules

Raymond, BBA

Jenkins, C

Seymour, LM Tacchi, JL Widjaja, M

Jarocki, VM

Deutscher, AT Turnbull, L

Whitchurch, CB

Padula, MP

Djordjevic, SP

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Publication Type:: Journal Article
Citation:: Cellular Microbiology, 2015, 17 (3), pp. 425 - 444
Issue Date:: 2015-01-01

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Field	Value	Language
dc.contributor.author	Raymond, BBA https://orcid.org/0000-0003-3610-9289	en_US
dc.contributor.author	Jenkins, C https://orcid.org/0000-0002-5966-072X	en_US
dc.contributor.author	Seymour, LM	en_US
dc.contributor.author	Tacchi, JL	en_US
dc.contributor.author	Widjaja, M https://orcid.org/0000-0003-1509-0443	en_US
dc.contributor.author	Jarocki, VM https://orcid.org/0000-0003-1249-0994	en_US
dc.contributor.author	Deutscher, AT	en_US
dc.contributor.author	Turnbull, L https://orcid.org/0000-0002-9255-9033	en_US
dc.contributor.author	Whitchurch, CB https://orcid.org/0000-0003-2296-3791	en_US
dc.contributor.author	Padula, MP https://orcid.org/0000-0002-8283-0643	en_US
dc.contributor.author	Djordjevic, SP https://orcid.org/0000-0001-9301-5372	en_US
dc.date.available	2014-10-03	en_US
dc.date.issued	2015-01-01	en_US
dc.identifier.citation	Cellular Microbiology, 2015, 17 (3), pp. 425 - 444	en_US
dc.identifier.issn	1462-5814	en_US
dc.identifier.uri	http://hdl.handle.net/10453/37997
dc.description.abstract	© 2014 John Wiley & Sons Ltd. Summary: Mycoplasma hyopneumoniae, the aetiological agent of porcine enzootic pneumonia, regulates the presentation of proteins on its cell surface via endoproteolysis, including those of the cilial adhesin P123 (MHJ_0194). These proteolytic cleavage events create functional adhesins that bind to proteoglycans and glycoproteins on the surface of ciliated and non-ciliated epithelial cells and to the circulatory host molecule plasminogen. Two dominant cleavage events of the P123 preprotein have been previously characterized; however, immunoblotting studies suggest that more complex processing events occur. These extensive processing events are characterized here. The functional significance of the P97 cleavage fragments is also poorly understood. Affinity chromatography using heparin, fibronectin and plasminogen as bait and peptide arrays were used to expand our knowledge of the adhesive capabilities of P123 cleavage fragments and characterize a novel binding motif in the C-terminus of P123. Further, we use immunohistochemistry to examine in vivo, the biological significance of interactions between M.hyopneumoniae and fibronectin and show that M.hyopneumoniae induces fibronectin deposition at the site of infection on the ciliated epithelium. Our data supports the hypothesis that M. hyopneumoniae possesses the molecular machinery to influence key molecular communication pathways in host cells.	en_US
dc.relation.ispartof	Cellular Microbiology	en_US
dc.relation.isbasedon	10.1111/cmi.12377	en_US
dc.subject.classification	Microbiology	en_US
dc.subject.mesh	Mycoplasma hyopneumoniae	en_US
dc.subject.mesh	Glycoproteins	en_US
dc.subject.mesh	Polysaccharides	en_US
dc.subject.mesh	Adhesins, Bacterial	en_US
dc.subject.mesh	Fibronectins	en_US
dc.subject.mesh	Immunoblotting	en_US
dc.subject.mesh	Chromatography, Affinity	en_US
dc.subject.mesh	Electrophoresis, Gel, Two-Dimensional	en_US
dc.subject.mesh	Protein Array Analysis	en_US
dc.subject.mesh	Immunohistochemistry	en_US
dc.subject.mesh	Protein Processing, Post-Translational	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	Tandem Mass Spectrometry	en_US
dc.subject.mesh	Protein Interaction Domains and Motifs	en_US
dc.subject.mesh	Proteolysis	en_US
dc.title	Proteolytic processing of the cilium adhesin MHJ_0194 (P123<inf>J</inf>) in Mycoplasma hyopneumoniae generates a functionally diverse array of cleavage fragments that bind multiple host molecules	en_US
dc.type	Journal Article
utslib.citation.volume	3	en_US
utslib.citation.volume	17	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	3	en_US
pubs.publication-status	Published	en_US
pubs.volume	17	en_US

Abstract:

© 2014 John Wiley & Sons Ltd. Summary: Mycoplasma hyopneumoniae, the aetiological agent of porcine enzootic pneumonia, regulates the presentation of proteins on its cell surface via endoproteolysis, including those of the cilial adhesin P123 (MHJ_0194). These proteolytic cleavage events create functional adhesins that bind to proteoglycans and glycoproteins on the surface of ciliated and non-ciliated epithelial cells and to the circulatory host molecule plasminogen. Two dominant cleavage events of the P123 preprotein have been previously characterized; however, immunoblotting studies suggest that more complex processing events occur. These extensive processing events are characterized here. The functional significance of the P97 cleavage fragments is also poorly understood. Affinity chromatography using heparin, fibronectin and plasminogen as bait and peptide arrays were used to expand our knowledge of the adhesive capabilities of P123 cleavage fragments and characterize a novel binding motif in the C-terminus of P123. Further, we use immunohistochemistry to examine in vivo, the biological significance of interactions between M.hyopneumoniae and fibronectin and show that M.hyopneumoniae induces fibronectin deposition at the site of infection on the ciliated epithelium. Our data supports the hypothesis that M. hyopneumoniae possesses the molecular machinery to influence key molecular communication pathways in host cells.

Please use this identifier to cite or link to this item:

http://hdl.handle.net/10453/37997