P159 from Mycoplasma hyopneumoniae binds porcine cilia and heparin and is cleaved in a manner akin to ectodomain shedding

Raymond, BBA; Tacchi, JL; Jarocki, VM; Minion, FC; Padula, MP; Djordjevic, SP

P159 from Mycoplasma hyopneumoniae binds porcine cilia and heparin and is cleaved in a manner akin to ectodomain shedding

Raymond, BBA

Tacchi, JL Jarocki, VM

Minion, FC Padula, MP

Djordjevic, SP

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Publication Type:: Journal Article
Citation:: Journal of Proteome Research, 2013, 12 (12), pp. 5891 - 5903
Issue Date:: 2013-12-06

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Field	Value	Language
dc.contributor.author	Raymond, BBA https://orcid.org/0000-0003-3610-9289	en_US
dc.contributor.author	Tacchi, JL	en_US
dc.contributor.author	Jarocki, VM https://orcid.org/0000-0003-1249-0994	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	2013-12-06	en_US
dc.identifier.citation	Journal of Proteome Research, 2013, 12 (12), pp. 5891 - 5903	en_US
dc.identifier.issn	1535-3893	en_US
dc.identifier.uri	http://hdl.handle.net/10453/26516
dc.description.abstract	Mycoplasma hyopneumoniae colonizes the ciliated epithelial lining of the upper respiratory tract of swine and results in chronic infection. Previously, we have observed that members of P97 and P102 paralog families of cilium adhesins undergo endoproteolytic processing on the surface of M. hyopneumoniae. We show that P159 (MHJ-0494), an epithelial cell adhesin unrelated to P97 and P102 paralog families, is a cilium adhesin that undergoes dominant cleavage events at S/T-X-F↓X-D/E-like motifs located at positions 233F↓Q234 and 981F↓Q982, generating P27, P110, and P52. An unrelated cleavage site 738L-K- V↓G-A-A743 in P110 shows sequence identity with a cleavage site (L-N-V↓A-V-S) identified in the P97 paralog, Mhp385, and generates 76 (P76) and 35 kDa (P35) fragments. LC-MS/MS analysis of biotinylated surface proteins identified six peptides with a biotin moiety on their N-terminus indicating novel, low abundance neo-N-termini. LC-MS/MS of proteins separated by 2D-PAGE, 2D immunoblotting using monospecific antiserum raised against recombinant fragments spanning P159 (F1P159-F4P159), and proteins that bound to heparin-agarose were all used to map P159 cleavage fragments. P159 is the first cilium adhesin not belonging to the P97/P102 paralog families and is extensively processed in a manner akin to ectodomain shedding in eukaryotes. © 2013 American Chemical Society.	en_US
dc.relation.ispartof	Journal of Proteome Research	en_US
dc.relation.isbasedon	10.1021/pr400903s	en_US
dc.subject.classification	Biochemistry & Molecular Biology	en_US
dc.subject.mesh	Respiratory System	en_US
dc.subject.mesh	Cilia	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	Heparin	en_US
dc.subject.mesh	Peptide Fragments	en_US
dc.subject.mesh	Adhesins, Bacterial	en_US
dc.subject.mesh	Chromatography, Liquid	en_US
dc.subject.mesh	Peptide Mapping	en_US
dc.subject.mesh	Biotinylation	en_US
dc.subject.mesh	Binding Sites	en_US
dc.subject.mesh	Amino Acid Sequence	en_US
dc.subject.mesh	Protein Binding	en_US
dc.subject.mesh	Molecular Weight	en_US
dc.subject.mesh	Molecular Sequence Data	en_US
dc.subject.mesh	Tandem Mass Spectrometry	en_US
dc.subject.mesh	Proteolysis	en_US
dc.title	P159 from Mycoplasma hyopneumoniae binds porcine cilia and heparin and is cleaved in a manner akin to ectodomain shedding	en_US
dc.type	Journal Article
utslib.citation.volume	12	en_US
utslib.for	0605 Microbiology	en_US
utslib.for	03 Chemical Sciences	en_US
utslib.for	06 Biological Sciences	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	12	en_US
pubs.publication-status	Published	en_US
pubs.volume	12	en_US

Abstract:

Mycoplasma hyopneumoniae colonizes the ciliated epithelial lining of the upper respiratory tract of swine and results in chronic infection. Previously, we have observed that members of P97 and P102 paralog families of cilium adhesins undergo endoproteolytic processing on the surface of M. hyopneumoniae. We show that P159 (MHJ-0494), an epithelial cell adhesin unrelated to P97 and P102 paralog families, is a cilium adhesin that undergoes dominant cleavage events at S/T-X-F↓X-D/E-like motifs located at positions 233F↓Q234 and 981F↓Q982, generating P27, P110, and P52. An unrelated cleavage site 738L-K- V↓G-A-A743 in P110 shows sequence identity with a cleavage site (L-N-V↓A-V-S) identified in the P97 paralog, Mhp385, and generates 76 (P76) and 35 kDa (P35) fragments. LC-MS/MS analysis of biotinylated surface proteins identified six peptides with a biotin moiety on their N-terminus indicating novel, low abundance neo-N-termini. LC-MS/MS of proteins separated by 2D-PAGE, 2D immunoblotting using monospecific antiserum raised against recombinant fragments spanning P159 (F1P159-F4P159), and proteins that bound to heparin-agarose were all used to map P159 cleavage fragments. P159 is the first cilium adhesin not belonging to the P97/P102 paralog families and is extensively processed in a manner akin to ectodomain shedding in eukaryotes. © 2013 American Chemical Society.

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http://hdl.handle.net/10453/26516