Two domains within the Mycoplasma hyopneumoniae Cilium adnesis bind heparin

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dc.contributor.author Jenkins, Cheryl en_US
dc.contributor.author Wilton, Jody en_US
dc.contributor.author Minion, F. Chris en_US
dc.contributor.author Falconer, Delia en_US
dc.contributor.author Walker, Mark en_US
dc.contributor.author Djordjevic, Steven en_US
dc.contributor.editor en_US
dc.date.accessioned 2010-05-28T09:51:02Z
dc.date.available 2010-05-28T09:51:02Z
dc.date.issued 2006 en_US
dc.identifier 2008007092 en_US
dc.identifier.citation Jenkins Cheryl et al. 2006, 'Two domains within the Mycoplasma hyopneumoniae Cilium adnesis bind heparin', Amer Soc Microbiology, vol. 74, no. 1, pp. 481-487. en_US
dc.identifier.issn 0019-9567 en_US
dc.identifier.other C1UNSUBMIT en_US
dc.identifier.uri http://hdl.handle.net/10453/9658
dc.description.abstract 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 (Mhp183, P97) is intricately but not exclusively involved in this process. Although binding of pathogenic bacteria to glycosaminoglycans is a recognized step in pathogenesis, knowledge of glycosaminoglycan-binding proteins in M. hyopneumoniae is lacking. 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 within the cilium adhesin were examined for the ability to bind heparin. Cilium adhesin fragments comprising 653 amino acids of the N terminus and 301 amino acids of the C terminus (containing two repeat regions, R1 and R2) were cloned and expressed. These fragments bound heparin in a dose-dependent and saturable manner with physiologically significant binding affinities of 0.27 ? 0.02 ?M and 1.89 ? 0.33 ?M, respectively. Heparin binding of both fragments was strongly inhibited by the sulfated polysaccharides fucoidan and mucin but not by chondroitin sulfate B. en_US
dc.language en_US
dc.publisher Amer Soc Microbiology en_US
dc.relation.isbasedon http://dx.doi.org/10.1128/IAI.74.1.481-487.2006 en_US
dc.title Two domains within the Mycoplasma hyopneumoniae Cilium adnesis bind heparin en_US
dc.parent Infection And Immunity en_US
dc.journal.volume 74 en_US
dc.journal.number 1 en_US
dc.publocation Washington DC, USA en_US
dc.identifier.startpage 481 en_US
dc.identifier.endpage 487 en_US
dc.cauo.name SCI.Institute for Biotechnology of Infectious Diseases en_US
dc.conference Verified OK en_US
dc.for 060500 en_US
dc.personcode 117836 en_US
dc.personcode 0000052346 en_US
dc.personcode 0000052258 en_US
dc.personcode 034107 en_US
dc.personcode 0000041940 en_US
dc.personcode 107126 en_US
dc.percentage 100 en_US
dc.classification.name Microbiology 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 107126 en_US


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