P159 is a proteolytically processed, surface adhesin of Mycoplasma hyopneumoniae:defined domains of P159 bind heparin and promote adherence to eukaryote cells

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dc.contributor.author Burnett, T
dc.contributor.author Dinkla, K
dc.contributor.author Rohde, M
dc.contributor.author Chhatwal, G
dc.contributor.author Uphoff, C
dc.contributor.author Srivastava, M
dc.contributor.author Cordwell, SJ
dc.contributor.author Geary, S
dc.contributor.author Liao, X
dc.contributor.author Minion, F
dc.contributor.author Walker, M
dc.contributor.author Djordjevic, SP
dc.date.accessioned 2010-05-28T09:45:13Z
dc.date.issued 2006-01
dc.identifier.citation Molecular Microbiology, 2006, 60 (3), pp. 669 - 686
dc.identifier.issn 0950-382X
dc.identifier.other C1UNSUBMIT en_US
dc.identifier.uri http://hdl.handle.net/10453/8746
dc.description.abstract Mycoplasma hyopneumoniae, the causative agent of porcine enzootic pneumonia, colonizes 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 respiratory 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 four recombinant proteins spanning P159 (F1P159, F2P159, F3P159 and F4P159), only F3P159 and F4P159 bound heparin in a dose-dependent manner (Kd values 142.37 ± 22.01 nM; 75.37 ± 7.34 nM respectively). Scanning electron microscopic studies showed M. hyopneumoniae bound intimately to porcine kidney epithelial-like cells (PK15 cells) but these processes were inhibited by excess heparin and F4P159. Similarly, latex beads coated with F2P159 and F4P159 adhered to and entered PK15 cells, but heparin, F2P159 and F4P159 was inhibitory. These findings indicate that P159 is a post-translationally cleaved, glycosaminoglycan-binding adhesin of M. hyopneumoniae.
dc.publisher Blackwell Publishing Ltd
dc.relation.isbasedon 10.1111/j.1365-2958.2006.05139.x
dc.subject Microbiology
dc.subject Microbiology
dc.title P159 is a proteolytically processed, surface adhesin of Mycoplasma hyopneumoniae:defined domains of P159 bind heparin and promote adherence to eukaryote cells
dc.type Journal Article
dc.parent Molecular Microbiology
dc.journal.volume 3
dc.journal.volume 60
dc.journal.number 3 en_US
dc.publocation UK en_US
dc.identifier.startpage 669 en_US
dc.identifier.endpage 686 en_US
dc.cauo.name SCI.Institute for Biotechnology of Infectious Diseases en_US
dc.conference Verified OK en_US
dc.for 0707 Veterinary Sciences
dc.personcode 0000052312 en_US
dc.personcode 0000052313 en_US
dc.personcode 0000052314 en_US
dc.personcode 0000052315 en_US
dc.personcode 0000052316 en_US
dc.personcode 0000052317 en_US
dc.personcode 0000027041 en_US
dc.personcode 0000052302 en_US
dc.personcode 0000052318 en_US
dc.personcode 0000052258 en_US
dc.personcode 0000035449 en_US
dc.personcode 107126 en_US
dc.percentage 100 en_US
dc.classification.name Veterinary Sciences 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
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


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