Sequence TTKF | QE defines the site of proteolytic cleavage in Mhp683, a novel glycosaminoglycan and cilium adhesin of Mycoplasma hyopneumoniae

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dc.contributor.author Bogema, Daniel en_US
dc.contributor.author Scott, Nichollas en_US
dc.contributor.author Padula, Matthew en_US
dc.contributor.author Tacchi, Jessica en_US
dc.contributor.author Raymond, Benjamin 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 Walker, Mark en_US
dc.contributor.author Djordjevic, Steven en_US
dc.contributor.editor en_US
dc.date.accessioned 2012-10-12T03:33:30Z
dc.date.available 2012-10-12T03:33:30Z
dc.date.issued 2011 en_US
dc.identifier 2011001420 en_US
dc.identifier.citation Bogema Daniel et al. 2011, 'Sequence TTKF | QE defines the site of proteolytic cleavage in Mhp683, a novel glycosaminoglycan and cilium adhesin of Mycoplasma hyopneumoniae', ASBMB, vol. 286, no. 48, pp. 41217-41229. en_US
dc.identifier.issn 0021-9258 en_US
dc.identifier.other C1 en_US
dc.identifier.uri http://hdl.handle.net/10453/18178
dc.description.abstract Mycoplasma hyopneumoniae colonizes the ciliated respiratory epithelium of swine, disrupting mucociliary function and inducing chronic inflammation. P97 and P102 family members are major surface proteins of M. hyopneumoniae and play key roles in colonizing cilia via interactions with glycosaminoglycans and mucin. The p102 paralog, mhp683, and homologs in strains from different geographic origins encode a 135-kDa pre-protein (P135) that is cleaved into three fragments identified here as P45683, P48683, and P50683. A peptide sequence (TTKF?QE) was identified surrounding both cleavage sites in Mhp683. N-terminal sequences of P48683 and P50683, determined by Edman degradation and mass spectrometry, confirmed cleavage after the phenylalanine residue. A similar proteolytic cleavage site was identified by mass spectrometry in another paralog of the P97/P102 family. Trypsin digestion and surface biotinylation studies showed that P45683, P48683, and P50683 reside on the M. hyopneumoniae cell surface. Binding assays of recombinant proteins F1683?F5683, spanning Mhp683, showed saturable and dose-dependent binding to biotinylated heparin that was inhibited by unlabeled heparin, fucoidan, and mucin. F1683?F5683 also bound porcine epithelial cilia, and antisera to F2683 and F5683 significantly inhibited cilium binding by M. hyopneumoniae cells. These data suggest that P45683, P48683, and P50683 each display cilium- and proteoglycan-binding sites. Mhp683 is the first characterized glycosaminoglycan-binding member of the P102 family. en_US
dc.language en_US
dc.publisher ASBMB en_US
dc.relation.isbasedon http://dx.doi.org/10.1074/jbc.M111.226084 en_US
dc.title Sequence TTKF | QE defines the site of proteolytic cleavage in Mhp683, a novel glycosaminoglycan and cilium adhesin of Mycoplasma hyopneumoniae en_US
dc.parent Journal Of Biological Chemistry en_US
dc.journal.volume 286 en_US
dc.journal.number 48 en_US
dc.publocation USA en_US
dc.identifier.startpage 41217 en_US
dc.identifier.endpage 41229 en_US
dc.cauo.name SCI.Faculty of Science en_US
dc.conference Verified OK en_US
dc.for 060100 en_US
dc.personcode 0000073523 en_US
dc.personcode 0000052321 en_US
dc.personcode 970082 en_US
dc.personcode 10422780 en_US
dc.personcode 10577005 en_US
dc.personcode 117836 en_US
dc.personcode 0000027041 en_US
dc.personcode 0000052258 en_US
dc.personcode 0000073526 en_US
dc.personcode 107126 en_US
dc.percentage 50 en_US
dc.classification.name Biochemistry and Cell Biology 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 Adhesion Bacteria Heparin-binding Protein Protease Protein Motifs Protein Processing Mycoplasma hyopneumoniae P102 Cilium-binding Proteins en_US
dc.staffid 107126 en_US


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