Mhp493 (P216) is a proteolytically processed, cilium and heparin binding protein of Mycoplasma hyopneumoniae.

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Show simple item record Wilton, J Jenkins, C Cordwell, SJ Falconer, L Minion, FC Oneal, DC Djordjevic, MA Connolly, A Barchia, I Walker, MJ Djordjevic, SP 2012-02-02T08:41:49Z 2009-02
dc.identifier.citation Molecular microbiology, 2009, 71 (3), pp. 566 - 582
dc.identifier.issn 0950-382X
dc.identifier.other C1 en_US
dc.description.abstract Mycoplasma hyopneumoniae induces respiratory disease in swine by colonizing cilia causing ciliostasis, cilial loss and epithelial cell death. Heparin binds to M. hyopneumoniae cells in a dose-dependent manner and blocks its ability to adhere to porcine cilia. We show here that Mhp493 (P216), a paralogue of the cilium adhesin P97 (Mhp183), is cleaved between amino acids 1040 and 1089 generating surface-accessible, heparin-binding proteins P120 and P85. Antiphosphoserine antibodies recognized P85 in 2-D immunoblotting studies and TiO(2) chromatography of trypsin digests of P85 isolated a single peptide with an m/z of 917.3. A phosphoserine residue in the tryptic peptide (90)VSELpSFR(96) (position 94 in P85) was identified by MALDI-MS/MS. Polyhistidine fusion proteins (F1(P216), F2(P216), F3(P216)) spanning Mhp493 bound heparin with biologically significant Kd values, and heparin, fucoidan and mucin inhibited this interaction. Latex beads coated with F1(P216), F2(P216) and F3(P216) adhered to and entered porcine kidney epithelial-like (PK15) cell monolayers. Microtitre plate-based assays showed that sequences within P120 and P85 bind to porcine cilia and are recognized by serum antibodies elicited during infection by M. hyopneumoniae. Mhp493 contributes significantly to the surface architecture of M. hyopneumoniae and is the first cilium adhesin to be described that lacks an R1 cilium-binding domain.
dc.format Print-Electronic
dc.language eng
dc.relation.isbasedon 10.1111/j.1365-2958.2008.06546.x
dc.title Mhp493 (P216) is a proteolytically processed, cilium and heparin binding protein of Mycoplasma hyopneumoniae.
dc.type Journal Article
dc.parent Molecular microbiology
dc.journal.volume 3
dc.journal.volume 71
dc.journal.number 3 en_US
dc.publocation UK en_US
dc.identifier.startpage 566 en_US
dc.identifier.endpage 582 en_US SCI.Institute for Biotechnology of Infectious Diseases en_US
dc.conference Verified OK en_US
dc.for 0605 Microbiology
dc.personcode 107126
dc.personcode 117836
dc.percentage 100 en_US Microbiology en_US
dc.classification.type FOR-08 en_US
dc.edition en_US
dc.custom en_US en_US
dc.location.activity en_US
dc.description.keywords Animals
dc.description.keywords Cells, Cultured
dc.description.keywords Cilia
dc.description.keywords Mycoplasma hyopneumoniae
dc.description.keywords Heparin
dc.description.keywords Recombinant Proteins
dc.description.keywords Antibodies, Bacterial
dc.description.keywords Cloning, Molecular
dc.description.keywords Protein Binding
dc.description.keywords Amino Acid Sequence
dc.description.keywords Molecular Sequence Data
dc.description.keywords Adhesins, Bacterial
dc.description.keywords Swine
dc.description.keywords Genes, Bacterial
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
utslib.copyright.status Closed Access 2015-04-15 12:17:09.805752+10
pubs.consider-herdc true
utslib.collection.history Closed (ID: 3)

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