Post-translational processing targets functionally diverse proteins in Mycoplasma hyopneumoniae

Jessica L. Tacchi, Benjamin B A Raymond, Paul A. Haynes, Iain J. Berry, Michael Widjaja, Daniel R. Bogema, Lauren K. Woolley, Cheryl Jenkins, F. Chris Minion, Matthew P. Padula, Steven P. Djordjevic*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

37 Citations (Scopus)
22 Downloads (Pure)

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 endopro-teolytic 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.

Original languageEnglish
Article number150210
Pages (from-to)1-18
Number of pages18
JournalOpen Biology
Volume6
Issue number2
DOIs
Publication statusPublished - 1 Feb 2016

Bibliographical note

Copyright the Author(s) 2016. Version archived for private and non-commercial use with the permission of the author/s and according to publisher conditions. For further rights please contact the publisher.

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