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Post-translational processing targets functionally diverse proteins in Mycoplasma hyopneumoniae.
Tacchi, Jessica L; Raymond, Benjamin B A; Haynes, Paul A; Berry, Iain J; Widjaja, Michael; Bogema, Daniel R; Woolley, Lauren K; Jenkins, Cheryl; Minion, F Chris; Padula, Matthew P; Djordjevic, Steven P.
Affiliation
  • Tacchi JL; The ithree Institute, University of Technology Sydney, PO Box 123, Broadway, New South Wales 2007, Australia.
  • Raymond BB; The ithree Institute, University of Technology Sydney, PO Box 123, Broadway, New South Wales 2007, Australia.
  • Haynes PA; Department of Chemistry and Biomolecular Sciences, Macquarie University, North Ryde, New South Wales 2109, Australia.
  • Berry IJ; The ithree Institute, University of Technology Sydney, PO Box 123, Broadway, New South Wales 2007, Australia.
  • Widjaja M; The ithree Institute, University of Technology Sydney, PO Box 123, Broadway, New South Wales 2007, Australia.
  • Bogema DR; The ithree Institute, University of Technology Sydney, PO Box 123, Broadway, New South Wales 2007, Australia NSW Department of Primary Industries, Elizabeth Macarthur Agricultural Institute, Menangle, New South Wales 2568, Australia.
  • Woolley LK; NSW Department of Primary Industries, Elizabeth Macarthur Agricultural Institute, Menangle, New South Wales 2568, Australia School of Biological Sciences, University of Wollongong, Wollongong, New South Wales 2522, Australia.
  • Jenkins C; NSW Department of Primary Industries, Elizabeth Macarthur Agricultural Institute, Menangle, New South Wales 2568, Australia.
  • Minion FC; Department of Veterinary Microbiology and Preventative Medicine, Iowa State University, Ames, IA 50011, USA.
  • Padula MP; The ithree Institute, University of Technology Sydney, PO Box 123, Broadway, New South Wales 2007, Australia Proteomics Core Facility, University of Technology Sydney, PO Box 123, Broadway, New South Wales 2007, Australia.
  • Djordjevic SP; The ithree Institute, University of Technology Sydney, PO Box 123, Broadway, New South Wales 2007, Australia Proteomics Core Facility, University of Technology Sydney, PO Box 123, Broadway, New South Wales 2007, Australia steven.djordjevic@uts.edu.au.
Open Biol ; 6(2): 150210, 2016 Feb.
Article in En | MEDLINE | ID: mdl-26865024
ABSTRACT
Mycoplasma hyopneumoniae is a genome-reduced, cell wall-less, bacterial pathogen with a predicted coding capacity of less than 700 proteins and is one of the smallest self-replicating pathogens. The cell surface of M. hyopneumoniae is extensively modified by processing events that target the P97 and P102 adhesin families. Here, we present analyses of the proteome of M. hyopneumoniae-type strain J using protein-centric approaches (one- and two-dimensional GeLC-MS/MS) that enabled us to focus on global processing events in this species. While these approaches only identified 52% of the predicted proteome (347 proteins), our analyses identified 35 surface-associated proteins with widely divergent functions that were targets of unusual endoproteolytic processing events, including cell adhesins, lipoproteins and proteins with canonical functions in the cytosol that moonlight on the cell surface. Affinity chromatography assays that separately used heparin, fibronectin, actin and host epithelial cell surface proteins as bait recovered cleavage products derived from these processed proteins, suggesting these fragments interact directly with the bait proteins and display previously unrecognized adhesive functions. We hypothesize that protein processing is underestimated as a post-translational modification in genome-reduced bacteria and prokaryotes more broadly, and represents an important mechanism for creating cell surface protein diversity.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Protein Processing, Post-Translational / Mycoplasma hyopneumoniae Language: En Journal: Open Biol Year: 2016 Document type: Article Affiliation country: Australia

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Protein Processing, Post-Translational / Mycoplasma hyopneumoniae Language: En Journal: Open Biol Year: 2016 Document type: Article Affiliation country: Australia