What is it about?
This review article describes examples of proteases, which are proteins that cut up other proteins, with additional functions. These proteases are often predicted to be intracellular but have been found unexpectedly on the cell surface. The additional "moonlighting" functions include binding to host cells (act as adhesins), manipulating host receptors, folding or unfolding other proteins (act as chaperones), and commandeering host immune pathways to escape destruction. We also describe how mass spectrometry is used in identifying such moonlighting proteins.
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Why is it important?
Proteases that are surface exposed are often considered virulence factors. However, those predicted to be intracellular are often considered "housekeeping" proteins. However, we describe that some of these "housekeeping" proteins leave their intracellular homes to play important roles in host epithelial adhesion, tissue invasion and in modulating immune responses. We also provide a list of predicted intracellular proteases that have been found on the surface of a number of bacterial pathogens, providing an opportunity for future researchers to explore what they might be doing there.
Perspectives
Finding out what is on the surface of a bacteria is vital as current prediction software fails to identify numerous proteins actually found in surfaceome studies. While there is an active debate on how these proteins are transported to the surface, I think trying to ascertain their functions there is exciting and has implications for future therapeutic designs.
Dr Veronica M Jarocki
University of Technology Sydney
Read the Original
This page is a summary of: Non-proteolytic functions of microbial proteases increase pathological complexity, PROTEOMICS, February 2015, Wiley,
DOI: 10.1002/pmic.201400386.
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