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

¹ Department of Primary Industries, Elizabeth Macarthur Agricultural Institute, Camden, NSW 2570, Australia
² School of Biological Sciences, University of Wollongong, NSW, Australia
³ Center of Excellence for Vaccine Research, The University of Connecticut, Storrs, CT 06269-3089, USA
⁴ Department of Pathobiology and Veterinary Science, The University of Connecticut, Storrs, CT 06269-3089, USA

Correspondence
Steven P. Djordjevic
steve.djordjevic{at}dpi.nsw.gov.au

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.

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				C. Jenkins, R. Samudrala, S. J. Geary, and S. P. Djordjevic Structural and Functional Characterization of an Organic Hydroperoxide Resistance Protein from Mycoplasma gallisepticum J. Bacteriol., March 15, 2008; 190(6): 2206 - 2216. [Abstract] [Full Text] [PDF]