Mhp493 (P216) is a proteolytically processed, cilium and heparin binding protein of Mycoplasma hyopneumoniae

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dc.contributor.author Wilton, Jody en_US
dc.contributor.author Jenkins, Cheryl en_US
dc.contributor.author Cordwell, Stuart en_US
dc.contributor.author Minion, F. Chris en_US
dc.contributor.author Oneal, David en_US
dc.contributor.author Djordjevic, Michael en_US
dc.contributor.author Connolly, Angela en_US
dc.contributor.author Barchia, Idris en_US
dc.contributor.author Walker, Mark en_US
dc.contributor.author Djordjevic, Steven en_US
dc.contributor.author Falconer, Linda en_US
dc.contributor.editor en_US
dc.date.accessioned 2012-02-02T08:41:49Z
dc.date.available 2012-02-02T08:41:49Z
dc.date.issued 2009 en_US
dc.identifier 2008007081 en_US
dc.identifier.citation Wilton Jody et al. 2009, 'Mhp493 (P216) is a proteolytically processed, cilium and heparin binding protein of Mycoplasma hyopneumoniae', Blackwell Publishing Ltd, vol. 71, no. 3, pp. 566-582. en_US
dc.identifier.issn 0950-382X en_US
dc.identifier.other C1 en_US
dc.identifier.uri http://hdl.handle.net/10453/15027
dc.description.abstract Mycoplasma hyopneumoniae induces respiratory disease in swine by colonizing cilia causing ciliostasis, cilial loss and epithelial cell death. Heparin binds to M. hyopneumoniae cells in a dose-dependent manner and blocks its ability to adhere to porcine cilia. We show here that Mhp493 (P216), a paralogue of the cilium adhesin P97 (Mhp183), is cleaved between amino acids 1040 and 1089 generating surface-accessible, heparin-binding proteins P120 and P85. Antiphosphoserine antibodies recognized P85 in 2-D immunoblotting studies and TiO2 chromatography of trypsin digests of P85 isolated a single peptide with an m/z of 917.3. A phosphoserine residue in the tryptic peptide (90)VSELpSFR(96) (position 94 in P85) was identified by MALDI-MS/MS. Polyhistidine fusion proteins (F1(P216), F2(P216), F3(P216)) spanning Mhp493 bound heparin with biologically significant Kd values, and heparin, fucoidan and mucin inhibited this interaction. Latex beads coated with F1(P216), F2(P216) and F3(P216) adhered to and entered porcine kidney epithelial-like (PK15) cell monolayers. Microtitre plate-based assays showed that sequences within P120 and P85 bind to porcine cilia and are recognized by serum antibodies elicited during infection by M. hyopneumoniae. Mhp493 contributes significantly to the surface architecture of M. hyopneumoniae and is the first cilium adhesin to be described that lacks an R1 cilium-binding domain. en_US
dc.language en_US
dc.publisher Blackwell Publishing Ltd en_US
dc.relation.isbasedon http://dx.doi.org/10.1111/j.1365-2958.2008.06546.x en_US
dc.title Mhp493 (P216) is a proteolytically processed, cilium and heparin binding protein of Mycoplasma hyopneumoniae en_US
dc.parent Molecular Microbiology en_US
dc.journal.volume 71 en_US
dc.journal.number 3 en_US
dc.publocation UK en_US
dc.identifier.startpage 566 en_US
dc.identifier.endpage 582 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 0000052346 en_US
dc.personcode 117836 en_US
dc.personcode 0000027041 en_US
dc.personcode 0000052258 en_US
dc.personcode 0000052347 en_US
dc.personcode 0000027042 en_US
dc.personcode 0000052323 en_US
dc.personcode 0000052348 en_US
dc.personcode 0000041940 en_US
dc.personcode 107126 en_US
dc.personcode 0000111870 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 SIMPLE SEQUENCE REPEATS; ELECTRON-MICROSCOPY; COMPLETE GENOME; ADHESIN GENE; SPF PIGLETS; ADHERENCE; SWINE; IDENTIFICATION; PIGS; P97 en_US
dc.staffid 107126 en_US


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