Two domains within the Mycoplasma hyopneumoniae cilium adhesin bind heparin.

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dc.contributor.author Jenkins, C
dc.contributor.author Wilton, JL
dc.contributor.author Minion, FC
dc.contributor.author Falconer, L
dc.contributor.author Walker, MJ
dc.contributor.author Djordjevic, SP
dc.date.accessioned 2010-05-28T09:51:02Z
dc.date.issued 2006-01
dc.identifier.citation Infection and immunity, 2006, 74 (1), pp. 481 - 487
dc.identifier.issn 0019-9567
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 microM and 1.89 +/- 0.33 microM, respectively. Heparin binding of both fragments was strongly inhibited by the sulfated polysaccharides fucoidan and mucin but not by chondroitin sulfate B. When the C-terminal repeat regions R1 and R2 were cloned separately and expressed, heparin-binding activity was lost, suggesting that both regions are required for heparin binding. The ability of the cilium adhesin to bind heparin indicates that this molecule plays a multifunctional role in the adherence of M. hyopneumoniae to host respiratory surfaces and therefore has important implications with respect to the pathogenesis of this organism.
dc.format Print
dc.language eng
dc.relation.isbasedon 10.1128/iai.74.1.481-487.2006
dc.title Two domains within the Mycoplasma hyopneumoniae cilium adhesin bind heparin.
dc.type Journal Article
dc.parent Infection and immunity
dc.journal.volume 1
dc.journal.volume 74
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 0605 Microbiology
dc.personcode 107126
dc.personcode 117836
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 Animals
dc.description.keywords Respiratory Mucosa
dc.description.keywords Mycoplasma hyopneumoniae
dc.description.keywords Polysaccharides
dc.description.keywords Heparin
dc.description.keywords Mucins
dc.description.keywords Protein Structure, Tertiary
dc.description.keywords Protein Binding
dc.description.keywords Binding, Competitive
dc.description.keywords Amino Acid Sequence
dc.description.keywords Amino Acid Motifs
dc.description.keywords Molecular Sequence Data
dc.description.keywords Adhesins, Bacterial
dc.description.keywords Computational Biology
dc.description.keywords Swine
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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