Mycoplasma hyopneumoniae surface proteins Mhp385 and Mhp384 bind host cilia and glycosaminoglycans and are endoproteolytically processed by proteases that recognize different cleavage motifs

Deutscher, Ania T., Tacchi, Jessica L., Minion, F. Chris, Padula, Matthew P., Crossett, Ben, Bogema, Daniel R., Jenkins, Cheryl, Kuit, Tracey A., Walker, Mark J. and Djordjevic, Steven P. (2012) Mycoplasma hyopneumoniae surface proteins Mhp385 and Mhp384 bind host cilia and glycosaminoglycans and are endoproteolytically processed by proteases that recognize different cleavage motifs. Journal of Proteome Research, 11 3: 1924-1936. doi:10.1021/pr201115v


Author Deutscher, Ania T.
Tacchi, Jessica L.
Minion, F. Chris
Padula, Matthew P.
Crossett, Ben
Bogema, Daniel R.
Jenkins, Cheryl
Kuit, Tracey A.
Walker, Mark J.
Djordjevic, Steven P.
Title Mycoplasma hyopneumoniae surface proteins Mhp385 and Mhp384 bind host cilia and glycosaminoglycans and are endoproteolytically processed by proteases that recognize different cleavage motifs
Formatted title
Mycoplasma hyopneumoniae surface proteins Mhp385 and Mhp384 bind host cilia and glycosaminoglycans and are endoproteolytically processed by proteases that recognize different cleavage motifs
Journal name Journal of Proteome Research   Check publisher's open access policy
ISSN 1535-3893
1535-3907
Publication date 2012-03-02
Sub-type Article (original research)
DOI 10.1021/pr201115v
Volume 11
Issue 3
Start page 1924
End page 1936
Total pages 13
Place of publication Washington, DC, United States
Publisher American Chemical Society
Collection year 2013
Language eng
Formatted abstract
P97 and P102 paralogues occur as endoproteolytic cleavage fragments on the surface of Mycoplasma hyopneumoniae that bind glycosaminoglycans, plasminogen, and fibronectin and perform essential roles in colonization of ciliated epithelia. We show that the P102 paralogue Mhp384 is efficiently cleaved at an S/T-X-F↓X-D/E-like site, creating P60384 and P50384. The P97 paralogue Mhp385 is inefficiently cleaved, with tryptic peptides from a 115 kDa protein (P115385) and 88 kDa (P88385) and 27 kDa (P27385) cleavage fragments identified by LC–MS/MS. This is the first time a preprotein belonging to the P97 and P102 paralogue families has been identified by mass spectrometry. The semitryptic peptide 752IQFELEPISLNV763 denotes the C-terminus of P88385 and defines the novel cleavage site 761L-N-V↓A-V-S766 in Mhp385. P115385, P88385, P27385, P60384, and P50384 were shown to reside extracellularly, though it is unknown how the fragments remain attached to the cell surface. Heparin- and cilium-binding sites were identified within P60384, P50384, and P88385. No primary function was attributed to P27385; however, this molecule contains four tandem R1 repeats with similarity to porcine collagen type VI (α3 chain). P97 and P102 paralogue families are adhesins targeted by several proteases with different cleavage efficiencies, and this process generates combinatorial complexity on the surface of M. hyopneumoniae.
Keyword Mycoplasma hyopneumoniae
Paralogue
Endoproteolytic cleavage
Cilium adhesin
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2013 Collection
School of Chemistry and Molecular Biosciences
 
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Created: Thu, 22 Mar 2012, 08:31:28 EST by Lucy O'Brien on behalf of School of Chemistry & Molecular Biosciences