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

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dc.contributor.author Jenkins, Cheryl en_US
dc.contributor.author Geary, Steven en_US
dc.contributor.author Gladd, Martha en_US
dc.contributor.author Djordjevic, Steven en_US
dc.contributor.editor en_US
dc.date.accessioned 2010-05-28T09:44:22Z
dc.date.available 2010-05-28T09:44:22Z
dc.date.issued 2007 en_US
dc.identifier 2008007064 en_US
dc.identifier.citation Jenkins Cheryl et al. 2007, 'The Mycoplasma gallisepticum OsmC-like protein MG1142 resides on the cell surace and binds heparin', Society for General Microbiology, vol. 153, pp. 1455-1463. en_US
dc.identifier.issn 1350-0872 en_US
dc.identifier.other C1UNSUBMIT 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. en_US
dc.language en_US
dc.publisher Society for General Microbiology en_US
dc.relation.isbasedon http://dx.doi.org/10.1099/mic.0.2006/004937-0 en_US
dc.title The Mycoplasma gallisepticum OsmC-like protein MG1142 resides on the cell surface and binds heparin en_US
dc.parent Microbiology-uk en_US
dc.journal.volume 153 en_US
dc.journal.number en_US
dc.publocation United Kingdom en_US
dc.identifier.startpage 1455 en_US
dc.identifier.endpage 1463 en_US
dc.cauo.name SCI.Institute for Biotechnology of Infectious Diseases en_US
dc.conference Verified OK en_US
dc.for 060800 en_US
dc.personcode 117836 en_US
dc.personcode 0000052302 en_US
dc.personcode 0000052303 en_US
dc.personcode 107126 en_US
dc.percentage 100 en_US
dc.classification.name Zoology en_US
dc.classification.type FOR-08 en_US
dc.edition en_US
dc.custom en_US
dc.date.activity en_US
dc.location.activity en_US
dc.description.keywords en_US
dc.staffid en_US
dc.staffid 107126 en_US


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