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

Article


Raymond, Benjamin B. A., Jenkins, Cheryl, Seymour, Lisa M., Tacchi, Jessica L., Widjaja, Michael, Jarocki, Veronica M., Deutscher, Ania T., Turnbull, Lynne, Whitchurch, Cynthia B., 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. https://doi.org/10.1111/cmi.12377
Article Title

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

ERA Journal ID2526
Article CategoryArticle
AuthorsRaymond, Benjamin B. A. (Author), Jenkins, Cheryl (Author), Seymour, Lisa M. (Author), Tacchi, Jessica L. (Author), Widjaja, Michael (Author), Jarocki, Veronica M. (Author), Deutscher, Ania T. (Author), Turnbull, Lynne (Author), Whitchurch, Cynthia B. (Author), Padula, Matthew P. (Author) and Djordjevic, Steven P. (Author)
Journal TitleCellular Microbiology
Journal Citation17 (3), pp. 425-444
Number of Pages20
Year2014
Place of PublicationUnited Kingdom
ISSN1462-5814
1462-5822
Digital Object Identifier (DOI)https://doi.org/10.1111/cmi.12377
Web Address (URL)http://onlinelibrary.wiley.com/doi/10.1111/cmi.12377/epdf
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.

ANZSRC Field of Research 2020300999. Veterinary sciences not elsewhere classified
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Byline AffiliationsUniversity of Technology Sydney
Elizabeth Macarthur Agricultural Institute, Australia
University of Wollongong
Institution of OriginUniversity of Southern Queensland
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https://research.usq.edu.au/item/q2y16/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

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