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

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dc.contributor.author Bogema, DR
dc.contributor.author Scott, NE
dc.contributor.author Padula, MP
dc.contributor.author Tacchi, JL
dc.contributor.author Raymond, BBA
dc.contributor.author Jenkins, C
dc.contributor.author Cordwell, SJ
dc.contributor.author Minion, FC
dc.contributor.author Walker, MJ
dc.contributor.author Djordjevic, SP
dc.date.accessioned 2012-10-12T03:33:30Z
dc.date.issued 2011-12-02
dc.identifier.citation Journal of Biological Chemistry, 2011, 286 (48), pp. 41217 - 41229
dc.identifier.issn 0021-9258
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 preprotein (P135) that is cleaved into three fragments identified here as P45 683, P48 683, and P50 683. A peptide sequence (TTKF ↓ QE) was identified surrounding both cleavage sites in Mhp683. N-terminal sequences of P48 683 and P50 683, 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 P45 683, P48 683, and P50 683 reside on the M. hyopneumoniae cell surface. Binding assays of recombinant proteins F1 683-F5 683, spanning Mhp683, showed saturable and dose-dependent binding to biotinylated heparin that was inhibited by unlabeled heparin, fucoidan, and mucin. F1 683-F5 683 also bound porcine epithelial cilia, and antisera to F2 683 and F5 683 significantly inhibited cilium binding by M. hyopneumoniae cells. These data suggest that P45 683, P48 683, and P50 683 each display cilium- and proteoglycan-binding sites. Mhp683 is the first characterized glycosaminoglycan-binding member of the P102 family. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.
dc.language eng
dc.relation.isbasedon 10.1074/jbc.M111.226084
dc.title Sequence TTKF ↓ QE defines the site of proteolytic cleavage in Mhp683 protein, a novel glycosaminoglycan and cilium adhesin of Mycoplasma hyopneumoniae
dc.type Journal Article
dc.description.version Published
dc.parent Journal of Biological Chemistry
dc.journal.volume 48
dc.journal.volume 286
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 0707 Veterinary Sciences
dc.for 0605 Microbiology
dc.personcode 970082
dc.personcode 107126
dc.personcode 119529
dc.personcode 117836
dc.personcode 108199
dc.percentage 67 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 Adhesion Bacteria Heparin-binding Protein Protease Protein Motifs Protein Processing Mycoplasma hyopneumoniae P102 Cilium-binding Proteins en_US
dc.description.keywords Social Sciences
dc.description.keywords Education & Educational Research
dc.description.keywords EDUCATION & EDUCATIONAL RESEARCH
dc.description.keywords interactive whiteboard (IWB)
dc.description.keywords primary education
dc.description.keywords dialogic interactions
dc.description.keywords interactive whole-class technologies
dc.description.keywords ICT
dc.description.keywords NATIONAL LITERACY
dc.description.keywords WHITEBOARDS
dc.description.keywords PERCEPTIONS
dc.description.keywords STRATEGIES
dc.description.keywords Respiratory Mucosa
dc.description.keywords Cells, Cultured
dc.description.keywords Cilia
dc.description.keywords Animals
dc.description.keywords Swine
dc.description.keywords Mycoplasma hyopneumoniae
dc.description.keywords Glycosaminoglycans
dc.description.keywords Adhesins, Bacterial
dc.description.keywords Bacterial Adhesion
dc.description.keywords Amino Acid Motifs
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
pubs.organisational-group /University of Technology Sydney/Students


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