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P159 Is A Proteolytically Processed, Surface Adhesin Of Mycoplasma Hyopneumoniae: Defined Domains Of P159 Bind Heparin And Promote Adherence To Eukaryote Cells., T. A. Burnett, K. Dinkla, M. Rohde, G. S. Chhatwal, C. Uphoff, M. Srivasta, S. J. Cordwell, S. Geary, X. Liao, F. C. Minion, Mark J. Walker, S. P. Djordjevic
P159 Is A Proteolytically Processed, Surface Adhesin Of Mycoplasma Hyopneumoniae: Defined Domains Of P159 Bind Heparin And Promote Adherence To Eukaryote Cells., T. A. Burnett, K. Dinkla, M. Rohde, G. S. Chhatwal, C. Uphoff, M. Srivasta, S. J. Cordwell, S. Geary, X. Liao, F. C. Minion, Mark J. Walker, S. P. Djordjevic
Faculty of Science - Papers (Archive)
Mycoplasma hyopneumoniae, the causative agent of porcine enzootic pneumonia, colonises 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 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 4 recombinant proteins spanning …
Two Domains Within The Mycoplasma Hyopneumoniae Cilium Adhesin Bind Heparin, C. Jenkins, J. L. Wilton, F. C. Minion, L. Falconer, Mark J. Walker, S. P. Djordjevic
Two Domains Within The Mycoplasma Hyopneumoniae Cilium Adhesin Bind Heparin, C. Jenkins, J. L. Wilton, F. C. Minion, L. Falconer, Mark J. Walker, S. P. Djordjevic
Faculty of Science - Papers (Archive)
Mycoplasma hyopneumoniae is the causative agent of porcine enzootic pneumonia, a chronic and economically significant respiratory disease that affects swine production worldwide. M. hyopneumoniae adheres to, and adversely affects the function of ciliated epithelial cells of the respiratory tract, and the cilium adhesin (P97), is intricately but not exclusively involved in this process. Although binding of pathogenic bacteria to glycosaminoglycans is a recognised step in pathogenesis, knowledge of glycosaminoglycan-binding proteins is lacking in M. hyopneumoniae. However, heparin and other sulfated polysaccharides are known to block the binding of M. hyopneumoniae to purified swine respiratory cilia. In this study, four regions …