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

Raymond, Benjamin B. A. and Jenkins, Cheryl and Seymour, Lisa M. and Tacchi, Jessica L. and Widjaja, Michael and Jarocki, Veronica M. and Deutscher, Ania T. and Turnbull, Lynne and Whitchurch, Cynthia B. and Padula, Matthew P. and Djordjevic, Steven P. (2014) 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). pp. 425-444. ISSN 1462-5814

Abstract

[Summary]: 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.


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Item Type: Article (Commonwealth Reporting Category C)
Refereed: Yes
Item Status: Live Archive
Additional Information: Permanent restricted access to Published version, in accordance with the copyright policy of the publisher.
Faculty / Department / School: Historic - Faculty of Health, Engineering and Sciences - School of Health, Nursing and Midwifery
Date Deposited: 28 Apr 2016 04:36
Last Modified: 06 Sep 2016 01:46
Fields of Research : 07 Agricultural and Veterinary Sciences > 0707 Veterinary Sciences > 070707 Veterinary Microbiology (excl. Virology)
Socio-Economic Objective: B Economic Development > 83 Animal Production and Animal Primary Products > 8399 Other Animal Production and Animal Primary Products > 839999 Animal Production and Animal Primary Products not elsewhere classified
Identification Number or DOI: 10.1111/cmi.12377
URI: http://eprints.usq.edu.au/id/eprint/26909

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