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

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dc.contributor.author Jenkins, C
dc.contributor.author Geary, SJ
dc.contributor.author Gladd, M
dc.contributor.author Djordjevic, SP
dc.date.accessioned 2010-05-28T09:44:22Z
dc.date.issued 2007-05
dc.identifier.citation Microbiology (Reading, England), 2007, 153 (Pt 5), pp. 1455 - 1463
dc.identifier.issn 1350-0872
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 (K(d)) 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.
dc.format Print
dc.language eng
dc.relation.isbasedon 10.1099/mic.0.2006/004937-0
dc.title The Mycoplasma gallisepticum OsmC-like protein MG1142 resides on the cell surface and binds heparin.
dc.type Journal Article
dc.parent Microbiology (Reading, England)
dc.journal.volume Pt 5
dc.journal.volume 153
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 0608 Zoology
dc.personcode 107126
dc.personcode 117836
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 Humans
dc.description.keywords Fibroblasts
dc.description.keywords Mycoplasma gallisepticum
dc.description.keywords Bacterial Proteins
dc.description.keywords Polysaccharides
dc.description.keywords Chondroitin Sulfates
dc.description.keywords Dermatan Sulfate
dc.description.keywords Heparin
dc.description.keywords Mucins
dc.description.keywords Membrane Proteins
dc.description.keywords Protein Binding
pubs.embargo.period Not known
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 - i3
utslib.copyright.status Closed Access
utslib.copyright.date 2015-04-15 12:17:09.805752+10
pubs.consider-herdc false
utslib.collection.history Closed (ID: 3)


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