P159 is a proteolytically processed, surface adhesin of Mycoplasma hyopneumoniae: Defined domains of P159 bind heparin and promote adherence to eukaryote cells

Burnett, TA; Dinkla, K; Rohde, M; Chhatwal, GS; Uphoff, C; Srivastava, M; Cordwell, SJ; Geary, S; Liao, X; Minion, FC; Walker, MJ; Djordjevic, SP

P159 is a proteolytically processed, surface adhesin of Mycoplasma hyopneumoniae: Defined domains of P159 bind heparin and promote adherence to eukaryote cells

Burnett, TA Dinkla, K Rohde, M Chhatwal, GS Uphoff, C Srivastava, M Cordwell, SJ Geary, S Liao, X Minion, FC Walker, MJ Djordjevic, SP

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Publication Type:: Journal Article
Citation:: Molecular Microbiology, 2006, 60 (3), pp. 669 - 686
Issue Date:: 2006-05-01

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Field	Value	Language
dc.contributor.author	Burnett, TA	en_US
dc.contributor.author	Dinkla, K	en_US
dc.contributor.author	Rohde, M	en_US
dc.contributor.author	Chhatwal, GS	en_US
dc.contributor.author	Uphoff, C	en_US
dc.contributor.author	Srivastava, M	en_US
dc.contributor.author	Cordwell, SJ	en_US
dc.contributor.author	Geary, S	en_US
dc.contributor.author	Liao, X	en_US
dc.contributor.author	Minion, FC	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	2006-05-01	en_US
dc.identifier.citation	Molecular Microbiology, 2006, 60 (3), pp. 669 - 686	en_US
dc.identifier.issn	0950-382X	en_US
dc.identifier.uri	http://hdl.handle.net/10453/8746
dc.description.abstract	Mycoplasma hyopneumoniae, the causative agent of porcine enzootic pneumonia, colonizes the respiratory cilia of affected swine causing significant economic losses to swine production worldwide. Heparin is known to inhibit adherence of M. hyopneumoniae to porcine respiratory epithelial cilia. M. hyopneumoniae cells bind heparin but the identity of the heparin-binding proteins is limited. Proteomic analysis of M. hyopneumoniae lysates identified 27 kDa (P27), 110 kDa (P110) and 52 kDa (P52) proteins representing different regions of a 159 kDa (P159) protein derived from mhp494. These cleavage fragments were surface located and present at all growth stages. Following purification of four recombinant proteins spanning P159 (F1P159, F2P159, F3P159 and F4P159), only F3 P159 and F4P159 bound heparin in a dose-dependent manner (Kd values 142.37 ± 22.01 nM; 75.37 ± 7.34 nM respectively). Scanning electron microscopic studies showed M. hyopneumoniae bound intimately to porcine kidney epithelial-like cells (PK15 cells) but these processes were inhibited by excess heparin and F4P159. Similarly, latex beads coated with F2P159 and F4P159 adhered to and entered PK15 cells, but heparin, F2P159 and F4P159 was inhibitory. These findings indicate that P159 is a post-translationally cleaved, glycosaminoglycan-binding adhesin of M. hyopneumoniae. © 2006 Blackwell Publishing Ltd.	en_US
dc.relation.ispartof	Molecular Microbiology	en_US
dc.relation.isbasedon	10.1111/j.1365-2958.2006.05139.x	en_US
dc.subject.classification	Microbiology	en_US
dc.subject.mesh	Kidney	en_US
dc.subject.mesh	Cell Line	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	Heparin	en_US
dc.subject.mesh	Adhesins, Bacterial	en_US
dc.subject.mesh	Recombinant Proteins	en_US
dc.subject.mesh	Bacterial Adhesion	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.title	P159 is a proteolytically processed, surface adhesin of Mycoplasma hyopneumoniae: Defined domains of P159 bind heparin and promote adherence to eukaryote cells	en_US
dc.type	Journal Article
utslib.citation.volume	3	en_US
utslib.citation.volume	60	en_US
utslib.for	0707 Veterinary Sciences	en_US
utslib.for	06 Biological Sciences	en_US
utslib.for	07 Agricultural and Veterinary Sciences	en_US
utslib.for	11 Medical and Health 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/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	60	en_US

Abstract:

Mycoplasma hyopneumoniae, the causative agent of porcine enzootic pneumonia, colonizes the respiratory cilia of affected swine causing significant economic losses to swine production worldwide. Heparin is known to inhibit adherence of M. hyopneumoniae to porcine respiratory epithelial cilia. M. hyopneumoniae cells bind heparin but the identity of the heparin-binding proteins is limited. Proteomic analysis of M. hyopneumoniae lysates identified 27 kDa (P27), 110 kDa (P110) and 52 kDa (P52) proteins representing different regions of a 159 kDa (P159) protein derived from mhp494. These cleavage fragments were surface located and present at all growth stages. Following purification of four recombinant proteins spanning P159 (F1P159, F2P159, F3P159 and F4P159), only F3 P159 and F4P159 bound heparin in a dose-dependent manner (Kd values 142.37 ± 22.01 nM; 75.37 ± 7.34 nM respectively). Scanning electron microscopic studies showed M. hyopneumoniae bound intimately to porcine kidney epithelial-like cells (PK15 cells) but these processes were inhibited by excess heparin and F4P159. Similarly, latex beads coated with F2P159 and F4P159 adhered to and entered PK15 cells, but heparin, F2P159 and F4P159 was inhibitory. These findings indicate that P159 is a post-translationally cleaved, glycosaminoglycan-binding adhesin of M. hyopneumoniae. © 2006 Blackwell Publishing Ltd.

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http://hdl.handle.net/10453/8746