Post-translational processing targets functionally diverse proteins in Mycoplasma hyopneumoniae

Tacchi, JL; Raymond, BBA; Haynes, PA; Berry, IJ; Widjaja, M; Bogema, DR; Woolley, LK; Jenkins, C; Minion, FC; Padula, MP; Djordjevic, SP

Post-translational processing targets functionally diverse proteins in Mycoplasma hyopneumoniae

Tacchi, JL Raymond, BBA

Haynes, PA Berry, IJ

Widjaja, M

Bogema, DR

Woolley, LK Jenkins, C

Minion, FC Padula, MP

Djordjevic, SP

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Publication Type:: Journal Article
Citation:: Open Biology, 2016, 6 (2)
Issue Date:: 2016-02-01

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Field	Value	Language
dc.contributor.author	Tacchi, JL	en_US
dc.contributor.author	Raymond, BBA https://orcid.org/0000-0003-3610-9289	en_US
dc.contributor.author	Haynes, PA	en_US
dc.contributor.author	Berry, IJ https://orcid.org/0000-0002-0322-2595	en_US
dc.contributor.author	Widjaja, M https://orcid.org/0000-0003-1509-0443	en_US
dc.contributor.author	Bogema, DR https://orcid.org/0000-0001-7013-7326	en_US
dc.contributor.author	Woolley, LK	en_US
dc.contributor.author	Jenkins, C https://orcid.org/0000-0002-5966-072X	en_US
dc.contributor.author	Minion, FC	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.issued	2016-02-01	en_US
dc.identifier.citation	Open Biology, 2016, 6 (2)	en_US
dc.identifier.uri	http://hdl.handle.net/10453/41593
dc.description.abstract	© 2016 The Authors. Mycoplasma hyopneumoniae is a genome-reduced, cell wall-less, bacterial pathogen with a predicted coding capacity of less than 700 proteins and is one of the smallest self-replicating pathogens. The cell surface of M. hyopneumoniae is extensively modified by processing events that target the P97 and P102 adhesin families. Here, we present analyses of the proteome of M. hyopneumoniae-type strain J using protein-centric approaches (one- and two-dimensional GeLC-MS/MS) that enabled us to focus on global processing events in this species. While these approaches only identified 52% of the predicted proteome (347 proteins), our analyses identified 35 surface-associated proteins with widely divergent functions that were targets of unusual endopro-teolytic processing events, including cell adhesins, lipoproteins and proteins with canonical functions in the cytosol that moonlight on the cell surface. Affinity chromatography assays that separately used heparin, fibronectin, actin and host epithelial cell surface proteins as bait recovered cleavage products derived from these processed proteins, suggesting these fragments interact directly with the bait proteins and display previously unrecognized adhesive functions. We hypothesize that protein processing is underestimated as a post-translational modification in genome-reduced bacteria and prokaryotes more broadly, and represents an important mechanism for creating cell surface protein diversity.	en_US
dc.relation.ispartof	Open Biology	en_US
dc.relation.isbasedon	10.1098/rsob.150210	en_US
dc.subject.mesh	Mycoplasma hyopneumoniae	en_US
dc.subject.mesh	Bacterial Proteins	en_US
dc.subject.mesh	Membrane Proteins	en_US
dc.subject.mesh	Proteome	en_US
dc.subject.mesh	Proteomics	en_US
dc.subject.mesh	Protein Processing, Post-Translational	en_US
dc.subject.mesh	Amino Acid Sequence	en_US
dc.subject.mesh	Molecular Sequence Data	en_US
dc.subject.mesh	Proteolysis	en_US
dc.title	Post-translational processing targets functionally diverse proteins in Mycoplasma hyopneumoniae	en_US
dc.type	Journal Article
utslib.citation.volume	2	en_US
utslib.citation.volume	6	en_US
utslib.for	060114 Systems Biology	en_US
utslib.for	060109 Proteomics and Intermolecular Interactions (excl. Medical Proteomics)	en_US
utslib.for	0605 Microbiology	en_US
utslib.for	0601 Biochemistry and Cell Biology	en_US
utslib.for	1107 Immunology	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	open_access
pubs.issue	2	en_US
pubs.publication-status	Published	en_US
pubs.volume	6	en_US

Abstract:

© 2016 The Authors. Mycoplasma hyopneumoniae is a genome-reduced, cell wall-less, bacterial pathogen with a predicted coding capacity of less than 700 proteins and is one of the smallest self-replicating pathogens. The cell surface of M. hyopneumoniae is extensively modified by processing events that target the P97 and P102 adhesin families. Here, we present analyses of the proteome of M. hyopneumoniae-type strain J using protein-centric approaches (one- and two-dimensional GeLC-MS/MS) that enabled us to focus on global processing events in this species. While these approaches only identified 52% of the predicted proteome (347 proteins), our analyses identified 35 surface-associated proteins with widely divergent functions that were targets of unusual endopro-teolytic processing events, including cell adhesins, lipoproteins and proteins with canonical functions in the cytosol that moonlight on the cell surface. Affinity chromatography assays that separately used heparin, fibronectin, actin and host epithelial cell surface proteins as bait recovered cleavage products derived from these processed proteins, suggesting these fragments interact directly with the bait proteins and display previously unrecognized adhesive functions. We hypothesize that protein processing is underestimated as a post-translational modification in genome-reduced bacteria and prokaryotes more broadly, and represents an important mechanism for creating cell surface protein diversity.

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http://hdl.handle.net/10453/41593