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

Bogema, Daniel R., Scott, Nichollas E., Padula, Matthew P., Tacchi, Jessica L., Raymond, Benjamin B. A., Jenkins, Cheryl, Cordwell, Stuart J., Minion, F. Chris, Walker, Mark J. and Djordjevic, Steven P. (2011) Sequence TTKF (down arrow) QE defines the site of proteolytic cleavage in Mhp683 protein, a novel glycosaminoglycan and cilium adhesin of Mycoplasma hyopneumoniae. Journal of Biological Chemistry, 286 48: 41217-41229. doi:10.1074/jbc.M111.226084

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Author Bogema, Daniel R.
Scott, Nichollas E.
Padula, Matthew P.
Tacchi, Jessica L.
Raymond, Benjamin B. A.
Jenkins, Cheryl
Cordwell, Stuart J.
Minion, F. Chris
Walker, Mark J.
Djordjevic, Steven P.
Title Sequence TTKF (down arrow) QE defines the site of proteolytic cleavage in Mhp683 protein, a novel glycosaminoglycan and cilium adhesin of Mycoplasma hyopneumoniae
Formatted title
Sequence TTKF ↓ QE defines the site of proteolytic cleavage in Mhp683 protein, a novel glycosaminoglycan and cilium adhesin of Mycoplasma hyopneumoniae
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
1083-351X
Publication date 2011-12-02
Year available 2011
Sub-type Article (original research)
DOI 10.1074/jbc.M111.226084
Open Access Status File (Publisher version)
Volume 286
Issue 48
Start page 41217
End page 41229
Total pages 13
Place of publication Bethesda, MD, U.S.A.
Publisher American Society for Biochemistry and Molecular Biology
Collection year 2012
Language eng
Formatted 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.
Keyword Adhesion
Bacteria
Heparin-binding protein
Protease
Protein motifs
Protein processing
Mycoplasma hyopneumoniae
P102
Cilium-binding proteins
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2012 Collection
School of Chemistry and Molecular Biosciences
 
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Created: Thu, 23 Feb 2012, 12:52:33 EST by Lucy O'Brien on behalf of School of Chemistry & Molecular Biosciences