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Post-translational processing targets functionally diverse proteins in Mycoplasma hyopneumoniae.
Jessica L Tacchi1, Benjamin B A Raymond1, Paul A Haynes2
1The ithree Institute, University of Technology Sydney, PO Box 123, Broadway, New South Wales 2007, Australia.
Open Biology
|February 12, 2016
Summary
Protein processing in Mycoplasma hyopneumoniae creates diverse cell surface proteins, revealing new adhesive functions. This mechanism is crucial for understanding genome-reduced bacteria.
Area of Science:
- Microbiology
- Bacterial Pathogenesis
- Proteomics
Background:
- Mycoplasma hyopneumoniae is a minimal genome bacterium and a significant swine pathogen.
- Its cell surface is modified by processing events targeting adhesin families like P97 and P102.
Purpose of the Study:
- To analyze the proteome of Mycoplasma hyopneumoniae strain J.
- To investigate global protein processing events and their impact on cell surface diversity.
Main Methods:
- Protein-centric proteomic analysis using one- and two-dimensional GeLC-MS/MS.
- Affinity chromatography assays with heparin, fibronectin, actin, and host cell surface proteins.
Main Results:
- Identified 35 surface-associated proteins targeted by endoproteolytic processing.
- Discovered cleavage products with previously unrecognized adhesive functions interacting with host proteins.
- Demonstrated protein processing as a key mechanism for cell surface diversity.
Conclusions:
- Protein processing is an underestimated post-translational modification in genome-reduced bacteria.
- This process generates significant cell surface protein diversity and novel adhesive functions in Mycoplasma hyopneumoniae.
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