Proteolytic processing of the cilium adhesin MHJ_0194 (P123J) in Mycoplasma hyopneumoniae generates a functionally diverse array of cleavage fragments that bind multiple host molecules

Authors

Benjamin Raymond, Ithree Institute, University of Technology Sydney
Cheryl Jenkins, NSW Department of Primary Industries
Lisa M. Seymour, University of WollongongFollow
Jessica Tacchi, University of Technology, Sydney
Michael Widjaja, University of Technology, Sydney
Veronica M. Jarocki, University of Technology, Sydney
Ania T. Deutscher, University of WollongongFollow
Lynne Turnbull, University of Technology, Sydney
Cynthia B. Whitchurch, University of Technology, Sydney
Matthew P. Padula, University of Technology, Sydney
Steven P. Djordjevic, University of Technology, Sydney

RIS ID

99452

Publication Details

Raymond, B. B. A., Jenkins, C., Seymour, L. M., Tacchi, J. L., Widjaja, M., Jarocki, V. M., Deutscher, A. T., Turnbull, L., Whitchurch, C. B., Padula, M. P. & Djordjevic, S. P. (2015). Proteolytic processing of the cilium adhesin MHJ_0194 (P123J) in Mycoplasma hyopneumoniae generates a functionally diverse array of cleavage fragments that bind multiple host molecules. Cellular Microbiology, 17 (3), 425-444.

Abstract

Mycoplasma hyopneumoniae, the aetiological agent of porcine enzootic pneumonia, regulates the presentation of proteins on its cell surface via endoproteolysis, including those of the cilial adhesin P123 (MHJ_0194). These proteolytic cleavage events create functional adhesins that bind to proteoglycans and glycoproteins on the surface of ciliated and non-ciliated epithelial cells and to the circulatory host molecule plasminogen. Two dominant cleavage events of the P123 preprotein have been previously characterized; however, immunoblotting studies suggest that more complex processing events occur. These extensive processing events are characterized here. The functional significance of the P97 cleavage fragments is also poorly understood. Affinity chromatography using heparin, fibronectin and plasminogen as bait and peptide arrays were used to expand our knowledge of the adhesive capabilities of P123 cleavage fragments and characterize a novel binding motif in the C-terminus of P123. Further, we use immunohistochemistry to examine in vivo, the biological significance of interactions between M. hyopneumoniae and fibronectin and show that M. hyopneumoniae induces fibronectin deposition at the site of infection on the ciliated epithelium. Our data supports the hypothesis that M. hyopneumoniae possesses the molecular machinery to influence key molecular communication pathways in host cells.