The Mycoplasma gallisepticum OsmC-like protein MG1142 resides on the cell surface and binds heparin

Jenkins, C; Geary, SJ; Gladd, M; Djordjevic, SP

The Mycoplasma gallisepticum OsmC-like protein MG1142 resides on the cell surface and binds heparin

Jenkins, C

Geary, SJ Gladd, M Djordjevic, SP

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Publication Type:: Journal Article
Citation:: Microbiology, 2007, 153 (5), pp. 1455 - 1463
Issue Date:: 2007-05-01

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Field	Value	Language
dc.contributor.author	Jenkins, C https://orcid.org/0000-0002-5966-072X	en_US
dc.contributor.author	Geary, SJ	en_US
dc.contributor.author	Gladd, M	en_US
dc.contributor.author	Djordjevic, SP https://orcid.org/0000-0001-9301-5372	en_US
dc.date.issued	2007-05-01	en_US
dc.identifier.citation	Microbiology, 2007, 153 (5), pp. 1455 - 1463	en_US
dc.identifier.issn	1350-0872	en_US
dc.identifier.uri	http://hdl.handle.net/10453/8604
dc.description.abstract	Mycoplasma gallisepticum is an avian pathogen that causes a chronic respiratory disease of chickens and results in significant economic losses to the poultry industry worldwide. Colonization of the host and the establishment of chronic disease are initiated by the cytadherence of M. gallisepticum to the host respiratory epithelium. While several proteins involved in cytadhesion have been characterized, molecules that interact with components of the host extracellular matrix, a process that is central to pathogenesis, are only now being identified. In this study, M. gallisepticum whole cells were shown to bind heparin in a specific and saturable manner. Heparin also significantly inhibited the binding of M. gallisepticum to the human lung fibroblast cell line MRC-5, suggesting a potential role for glycosaminoglycans (GAGs) in cytadherence. M. gallisepticum protein MG1142 (encoded by mga_1142), which displays homology to the osmotically induced (OsmC) family of proteins, binds strongly to heparin, is highly expressed during in vitro culture, and is surface accessible. Recombinant MG1142 bound heparin in a dose-dependent and saturable manner with a dissociation constant (Kd) of 10 ± 1.8 nM, which is within a physiologically significant range, compared to that of other heparin-binding proteins. Binding to heparin was inhibited by the heavily sulfated polysaccharide fucoidan, but not by mucin or chondroitin sulfate A or B, suggesting that electrostatic interactions between the sulfate groups of heparin and the positively charged basic residues of the MG1142 protein are important in binding. The ability of M. gallisepticum to bind GAGs may contribute to host adherence and colonization. © 2007 SGM.	en_US
dc.relation.ispartof	Microbiology	en_US
dc.relation.isbasedon	10.1099/mic.0.2006/004937-0	en_US
dc.subject.classification	Microbiology	en_US
dc.subject.mesh	Fibroblasts	en_US
dc.subject.mesh	Humans	en_US
dc.subject.mesh	Mycoplasma gallisepticum	en_US
dc.subject.mesh	Polysaccharides	en_US
dc.subject.mesh	Chondroitin Sulfates	en_US
dc.subject.mesh	Dermatan Sulfate	en_US
dc.subject.mesh	Heparin	en_US
dc.subject.mesh	Bacterial Proteins	en_US
dc.subject.mesh	Mucins	en_US
dc.subject.mesh	Membrane Proteins	en_US
dc.subject.mesh	Protein Binding	en_US
dc.title	The Mycoplasma gallisepticum OsmC-like protein MG1142 resides on the cell surface and binds heparin	en_US
dc.type	Journal Article
utslib.citation.volume	5	en_US
utslib.citation.volume	153	en_US
utslib.for	0608 Zoology	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	5	en_US
pubs.publication-status	Published	en_US
pubs.volume	153	en_US

Abstract:

Mycoplasma gallisepticum is an avian pathogen that causes a chronic respiratory disease of chickens and results in significant economic losses to the poultry industry worldwide. Colonization of the host and the establishment of chronic disease are initiated by the cytadherence of M. gallisepticum to the host respiratory epithelium. While several proteins involved in cytadhesion have been characterized, molecules that interact with components of the host extracellular matrix, a process that is central to pathogenesis, are only now being identified. In this study, M. gallisepticum whole cells were shown to bind heparin in a specific and saturable manner. Heparin also significantly inhibited the binding of M. gallisepticum to the human lung fibroblast cell line MRC-5, suggesting a potential role for glycosaminoglycans (GAGs) in cytadherence. M. gallisepticum protein MG1142 (encoded by mga_1142), which displays homology to the osmotically induced (OsmC) family of proteins, binds strongly to heparin, is highly expressed during in vitro culture, and is surface accessible. Recombinant MG1142 bound heparin in a dose-dependent and saturable manner with a dissociation constant (Kd) of 10 ± 1.8 nM, which is within a physiologically significant range, compared to that of other heparin-binding proteins. Binding to heparin was inhibited by the heavily sulfated polysaccharide fucoidan, but not by mucin or chondroitin sulfate A or B, suggesting that electrostatic interactions between the sulfate groups of heparin and the positively charged basic residues of the MG1142 protein are important in binding. The ability of M. gallisepticum to bind GAGs may contribute to host adherence and colonization. © 2007 SGM.

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http://hdl.handle.net/10453/8604