Mycoplasma hyopneumoniae surface proteins Mhp385 and Mhp384 bind host cilia and glycosaminoglycans and are endoproteolytically processed by proteases that recognize different cleavage motifs

Deutscher, AT; Tacchi, JL; Minion, FC; Padula, MP; Crossett, B; Bogema, DR; Jenkins, C; Kuit, TA; Walker, MJ; Djordjevic, SP

Mycoplasma hyopneumoniae surface proteins Mhp385 and Mhp384 bind host cilia and glycosaminoglycans and are endoproteolytically processed by proteases that recognize different cleavage motifs

Deutscher, AT Tacchi, JL Minion, FC Padula, MP

Crossett, B Bogema, DR

Jenkins, C

Kuit, TA Walker, MJ Djordjevic, SP

Permalink

Publication Type:: Journal Article
Citation:: Journal of Proteome Research, 2012, 11 (3), pp. 1924 - 1936
Issue Date:: 2012-03-02

Closed Access

	Filename	Description	Size
	2011001425OK.pdf		3.16 MB	Adobe PDF	View/Open

Copyright Clearance Process

Recently Added
In Progress
Closed Access

This item is closed access and not available.

Full metadata record

Field	Value	Language
dc.contributor.author	Deutscher, AT	en_US
dc.contributor.author	Tacchi, JL	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	Crossett, B	en_US
dc.contributor.author	Bogema, DR https://orcid.org/0000-0001-7013-7326	en_US
dc.contributor.author	Jenkins, C https://orcid.org/0000-0002-5966-072X	en_US
dc.contributor.author	Kuit, TA	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	2012-03-02	en_US
dc.identifier.citation	Journal of Proteome Research, 2012, 11 (3), pp. 1924 - 1936	en_US
dc.identifier.issn	1535-3893	en_US
dc.identifier.uri	http://hdl.handle.net/10453/18180
dc.description.abstract	P97 and P102 paralogues occur as endoproteolytic cleavage fragments on the surface of Mycoplasma hyopneumoniae that bind glycosaminoglycans, plasminogen, and fibronectin and perform essential roles in colonization of ciliated epithelia. We show that the P102 paralogue Mhp384 is efficiently cleaved at an S/T-X-F↓X-D/E-like site, creating P60 384 and P50 384. The P97 paralogue Mhp385 is inefficiently cleaved, with tryptic peptides from a 115 kDa protein (P115 385) and 88 kDa (P88 385) and 27 kDa (P27 385) cleavage fragments identified by LC-MS/MS. This is the first time a preprotein belonging to the P97 and P102 paralogue families has been identified by mass spectrometry. The semitryptic peptide 752IQFELEPISLNV 763 denotes the C-terminus of P88 385 and defines the novel cleavage site 761L-N-V↓A-V- S 766 in Mhp385. P115 385, P88 385, P27 385, P60 384, and P50 384 were shown to reside extracellularly, though it is unknown how the fragments remain attached to the cell surface. Heparin- and cilium-binding sites were identified within P60 384, P50 384, and P88 385. No primary function was attributed to P27 385; however, this molecule contains four tandem R1 repeats with similarity to porcine collagen type VI (α3 chain). P97 and P102 paralogue families are adhesins targeted by several proteases with different cleavage efficiencies, and this process generates combinatorial complexity on the surface of M. hyopneumoniae. © 2012 American Chemical Society.	en_US
dc.relation.ispartof	Journal of Proteome Research	en_US
dc.relation.isbasedon	10.1021/pr201115v	en_US
dc.subject.classification	Biochemistry & Molecular Biology	en_US
dc.subject.mesh	Trachea	en_US
dc.subject.mesh	Cells, Cultured	en_US
dc.subject.mesh	Cilia	en_US
dc.subject.mesh	Animals	en_US
dc.subject.mesh	Mycoplasma hyopneumoniae	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	Peptide Mapping	en_US
dc.subject.mesh	Bacterial Adhesion	en_US
dc.subject.mesh	Gene Expression	en_US
dc.subject.mesh	Binding Sites	en_US
dc.subject.mesh	Amino Acid Sequence	en_US
dc.subject.mesh	Amino Acid Motifs	en_US
dc.subject.mesh	Sequence Homology, Amino Acid	en_US
dc.subject.mesh	Operon	en_US
dc.subject.mesh	Molecular Sequence Data	en_US
dc.subject.mesh	Host-Pathogen Interactions	en_US
dc.subject.mesh	Proteolysis	en_US
dc.title	Mycoplasma hyopneumoniae surface proteins Mhp385 and Mhp384 bind host cilia and glycosaminoglycans and are endoproteolytically processed by proteases that recognize different cleavage motifs	en_US
dc.type	Journal Article
utslib.citation.volume	3	en_US
utslib.citation.volume	11	en_US
utslib.for	0605 Microbiology	en_US
utslib.for	03 Chemical Sciences	en_US
utslib.for	06 Biological Sciences	en_US
dc.location.activity	Amsterdam, NETHERLANDS
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	11	en_US

Abstract:

P97 and P102 paralogues occur as endoproteolytic cleavage fragments on the surface of Mycoplasma hyopneumoniae that bind glycosaminoglycans, plasminogen, and fibronectin and perform essential roles in colonization of ciliated epithelia. We show that the P102 paralogue Mhp384 is efficiently cleaved at an S/T-X-F↓X-D/E-like site, creating P60 384 and P50 384. The P97 paralogue Mhp385 is inefficiently cleaved, with tryptic peptides from a 115 kDa protein (P115 385) and 88 kDa (P88 385) and 27 kDa (P27 385) cleavage fragments identified by LC-MS/MS. This is the first time a preprotein belonging to the P97 and P102 paralogue families has been identified by mass spectrometry. The semitryptic peptide 752IQFELEPISLNV 763 denotes the C-terminus of P88 385 and defines the novel cleavage site 761L-N-V↓A-V- S 766 in Mhp385. P115 385, P88 385, P27 385, P60 384, and P50 384 were shown to reside extracellularly, though it is unknown how the fragments remain attached to the cell surface. Heparin- and cilium-binding sites were identified within P60 384, P50 384, and P88 385. No primary function was attributed to P27 385; however, this molecule contains four tandem R1 repeats with similarity to porcine collagen type VI (α3 chain). P97 and P102 paralogue families are adhesins targeted by several proteases with different cleavage efficiencies, and this process generates combinatorial complexity on the surface of M. hyopneumoniae. © 2012 American Chemical Society.

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

http://hdl.handle.net/10453/18180