Characterization of cleavage events in the multifunctional cilium adhesin Mhp684 (P146) reveals a mechanism by which Mycoplasma hyopneumoniae regulates surface topography

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dc.contributor.author Bogema, Daniel en_US
dc.contributor.author Deutscher, Ania en_US
dc.contributor.author Woolley, Lauren en_US
dc.contributor.author Seymour, Lisa en_US
dc.contributor.author Raymond, Benjamin en_US
dc.contributor.author Tacchi, Jessica en_US
dc.contributor.author Dixon, Nicholas en_US
dc.contributor.author Minion, F. Chris en_US
dc.contributor.author Jenkins, Cheryl en_US
dc.contributor.author Walker, Mark en_US
dc.contributor.author Djordjevic, Steven en_US
dc.contributor.author Padula, Matt en_US
dc.contributor.editor en_US
dc.date.accessioned 2012-10-12T03:33:24Z
dc.date.available 2012-10-12T03:33:24Z
dc.date.issued 2012 en_US
dc.identifier 2011004580 en_US
dc.identifier.citation Bogema Daniel et al. 2012, 'Characterization of cleavage events in the multifunctional cilium adhesin Mhp684 (P146) reveals a mechanism by which Mycoplasma hyopneumoniae regulates surface topography', American Society for Microbiology, vol. 3, no. 2, pp. e00282 en_US
dc.identifier.issn 2150-7511 en_US
dc.identifier.other C1 en_US
dc.identifier.uri http://hdl.handle.net/10453/18117
dc.description.abstract Mycoplasma hyopneumoniae causes enormous economic losses to swine production worldwide by colonizing the ciliated epithelium in the porcine respiratory tract, resulting in widespread damage to the mucociliary escalator, prolonged inflammation, reduced weight gain, and secondary infections. Protein Mhp684 (P146) comprises 1,317 amino acids, and while the N-terminal 400 residues display significant sequence identity to the archetype cilium adhesin P97, the remainder of the molecule is novel and displays unusual motifs. Proteome analysis shows that P146 preprotein is endogenously cleaved into three major fragments identified here as P50(P146), P40(P146), and P85(P146) that reside on the cell surface. Liquid chromatography with tandem mass spectrometry (LC-MS/MS) identified a semitryptic peptide that delineated a major cleavage site in Mhp684. Cleavage occurred at the phenylalanine residue within sequence (672)ATEF down arrow QQ(677), consistent with a cleavage motif resembling S/T-X-F down arrow X-D/E recently identified in Mhp683 and other P97/P102 family members. Biotinylated surface proteins recovered by avidin chromatography and separated by two-dimensional gel electrophoresis (2-D GE) showed that more-extensive endoproteolytic cleavage of P146 occurs. Recombinant fragments F1(P146)-F3(P146) that mimic P50(P146), P40(P146), and P85(P146) were constructed and shown to bind porcine epithelial cilia and biotinylated heparin with physiologically relevant affinity. Recombinant versions of F3(P146) generated from M. hyopneumoniae strain J and 232 sequences strongly bind porcine plasminogen, and the removal of their respective C-terminal lysine and arginine residues significantly reduces this interaction. These data reveal that P146 is an extensively processed, multifunctional adhesin of M. hyopneumoniae. Extensive cleavage coupled with variable cleavage efficiency provides a mechanism by which M. hyopneumoniae regulates protein topography. en_US
dc.language en_US
dc.publisher American Society for Microbiology en_US
dc.title Characterization of cleavage events in the multifunctional cilium adhesin Mhp684 (P146) reveals a mechanism by which Mycoplasma hyopneumoniae regulates surface topography en_US
dc.parent mBio en_US
dc.journal.volume 3 en_US
dc.journal.number 2 en_US
dc.publocation United States en_US
dc.identifier.startpage 1 en_US
dc.identifier.endpage en_US
dc.identifier.endpage 11 en_US
dc.cauo.name SCI.Faculty of Science en_US
dc.conference Verified OK en_US
dc.for 060500 en_US
dc.personcode 0000073523 en_US
dc.personcode 0000073528 en_US
dc.personcode 0000073530 en_US
dc.personcode 0000073527 en_US
dc.personcode 113696 en_US
dc.personcode 10422780 en_US
dc.personcode 970082 en_US
dc.personcode 0000066498 en_US
dc.personcode 0000052258 en_US
dc.personcode 117836 en_US
dc.personcode 0000073526 en_US
dc.personcode 107126 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 BIND HEPARIN; PLASMINOGEN-BINDING; COILED COILS; PROTEIN; SWINE; IDENTIFICATION; STRAINS; FIBRONECTIN; ADHERENCE; SEQUENCE en_US
dc.staffid 107126 en_US


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