Post-translational processing targets functionally diverse proteins in Mycoplasma hyopneumoniae
| Autor: | Benjamin B. A. Raymond, Daniel R. Bogema, F. Chris Minion, Jessica L. Tacchi, Paul A. Haynes, Matthew P. Padula, Lauren K. Woolley, Cheryl Jenkins, Michael Widjaja, Iain J. Berry, Steven P. Djordjevic |
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| Rok vydání: | 2016 |
| Předmět: |
Proteomics
0301 basic medicine Proteome Molecular Sequence Data Immunology Cell two-dimensional gels Biology global proteome General Biochemistry Genetics and Molecular Biology protein-centric Microbiology 03 medical and health sciences Bacterial Proteins Mycoplasma hyopneumoniae medicine Amino Acid Sequence lcsh:QH301-705.5 Peptide sequence Research Articles Actin Research General Neuroscience Membrane Proteins adhesins biology.organism_classification Cell biology Bacterial adhesin 030104 developmental biology medicine.anatomical_structure lcsh:Biology (General) Membrane protein Proteolysis processing Protein Processing Post-Translational |
| Zdroj: | Open Biology Open Biology, Vol 6, Iss 2 (2016) |
| ISSN: | 2046-2441 |
| DOI: | 10.1098/rsob.150210 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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