A proteolytically activated antimicrobial toxin encoded on a mobile plasmid of Bacteroidales induces a protective response

Jordan C. Evans, Valentina Laclare McEneany, Michael J. Coyne, Elizabeth P. Caldwell, Madeline L. Sheahan, Salena S. Von, Emily M. Coyne, Rodney K. Tweten () and Laurie E. Comstock ()
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Jordan C. Evans: University of Oklahoma Health Sciences Center
Valentina Laclare McEneany: Division of Infectious Diseases, Brigham and Women’s Hospital/Harvard Medical School
Michael J. Coyne: Division of Infectious Diseases, Brigham and Women’s Hospital/Harvard Medical School
Elizabeth P. Caldwell: University of Oklahoma Health Sciences Center
Madeline L. Sheahan: University of Chicago
Salena S. Von: Division of Infectious Diseases, Brigham and Women’s Hospital/Harvard Medical School
Emily M. Coyne: Division of Infectious Diseases, Brigham and Women’s Hospital/Harvard Medical School
Rodney K. Tweten: University of Oklahoma Health Sciences Center
Laurie E. Comstock: Division of Infectious Diseases, Brigham and Women’s Hospital/Harvard Medical School

Nature Communications, 2022, vol. 13, issue 1, 1-13

Abstract: Abstract Phocaeicola vulgatus is one of the most abundant and ubiquitous bacterial species of the human gut microbiota, yet a comprehensive analysis of antibacterial toxin production by members of this species has not been reported. Here, we identify and characterize a previously undescribed antibacterial protein. This toxin, designated BcpT, is encoded on a small mobile plasmid that is largely confined to strains of the closely related species Phocaeicola vulgatus and Phocaeicola dorei. BcpT is unusual in that it requires cleavage at two distinct sites for activation, and we identify bacterial proteases that perform this activation. We further identify BcpT’s receptor as the Lipid A-core glycan, allowing BcpT to target species of other Bacteroidales families. Exposure of cells to BcpT induces a response involving an unusual sigma/anti-sigma factor pair that is likely triggered by cell envelope stress, resulting in the expression of genes that partially protect cells from multiple antimicrobial toxins.

Date: 2022
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DOI: 10.1038/s41467-022-31925-w

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