Discovery of a proteolytic flagellin family in diverse bacterial phyla that assembles enzymatically active flagella

Ulrich Eckhard, Hina Bandukwala, Michael J. Mansfield, Giada Marino, Jiujun Cheng, Iain Wallace, Todd Holyoak, Trevor C. Charles, John Austin, Christopher M. Overall () and Andrew C. Doxey ()
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Ulrich Eckhard: University of British Columbia
Hina Bandukwala: University of Waterloo
Michael J. Mansfield: University of Waterloo
Giada Marino: University of British Columbia
Jiujun Cheng: University of Waterloo
Iain Wallace: University of Waterloo
Todd Holyoak: University of Waterloo
Trevor C. Charles: University of Waterloo
John Austin: Health Canada
Christopher M. Overall: University of British Columbia
Andrew C. Doxey: University of Waterloo

Nature Communications, 2017, vol. 8, issue 1, 1-9

Abstract: Abstract Bacterial flagella are cell locomotion and occasional adhesion organelles composed primarily of the polymeric protein flagellin, but to date have not been associated with any enzymatic function. Here, we report the bioinformatics-driven discovery of a class of enzymatic flagellins that assemble to form proteolytically active flagella. Originating by a metallopeptidase insertion into the central flagellin hypervariable region, this flagellin family has expanded to at least 74 bacterial species. In the pathogen, Clostridium haemolyticum, metallopeptidase-containing flagellin (which we termed flagellinolysin) is the second most abundant protein in the flagella and is localized to the extracellular flagellar surface. Purified flagellar filaments and recombinant flagellin exhibit proteolytic activity, cleaving nearly 1000 different peptides. With ~ 20,000 flagellin copies per ~ 10-μm flagella this assembles the largest proteolytic complex known. Flagellum-mediated extracellular proteolysis expands our understanding of the functional plasticity of bacterial flagella, revealing this family as enzymatic biopolymers that mediate interactions with diverse peptide substrates.

Date: 2017
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DOI: 10.1038/s41467-017-00599-0

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