Two domains within the Mycoplasma hyopneumoniae cilium adhesin bind heparin

Jenkins, Cheryl, Wilton, Jody L., Minion, F. Chris, Falconer, Linda, Walker, Mark J. and Djordjevic, Steven P. (2006) Two domains within the Mycoplasma hyopneumoniae cilium adhesin bind heparin. Infection and Immunity, 74 1: 481-487. doi:10.1128/IAI.74.1.481-487.2006

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Author Jenkins, Cheryl
Wilton, Jody L.
Minion, F. Chris
Falconer, Linda
Walker, Mark J.
Djordjevic, Steven P.
Title Two domains within the Mycoplasma hyopneumoniae cilium adhesin bind heparin
Journal name Infection and Immunity   Check publisher's open access policy
ISSN 1098-5522
Publication date 2006-01
Sub-type Article (original research)
DOI 10.1128/IAI.74.1.481-487.2006
Open Access Status File (Publisher version)
Volume 74
Issue 1
Start page 481
End page 487
Total pages 7
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Language eng
Formatted 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 µM and 1.89 ± 0.33 µM, 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.
Keyword Gene
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
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