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

Author

Listed:
  • 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
    University of Chicago)

  • 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
    University of Chicago)

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.

Suggested Citation

  • Jordan C. Evans & Valentina Laclare McEneany & Michael J. Coyne & Elizabeth P. Caldwell & Madeline L. Sheahan & Salena S. Von & Emily M. Coyne & Rodney K. Tweten & Laurie E. Comstock, 2022. "A proteolytically activated antimicrobial toxin encoded on a mobile plasmid of Bacteroidales induces a protective response," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-31925-w
    DOI: 10.1038/s41467-022-31925-w
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    References listed on IDEAS

    as
    1. Michael J. Coyne & Nathalie Béchon & Leigh M. Matano & Valentina Laclare McEneany & Maria Chatzidaki-Livanis & Laurie E. Comstock, 2019. "A family of anti-Bacteroidales peptide toxins wide-spread in the human gut microbiota," Nature Communications, Nature, vol. 10(1), pages 1-14, December.
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    Cited by:

    1. Hunter L. Abrahamsen & Tristan C. Sanford & Casie E. Collamore & Bronte A. Johnstone & Michael J. Coyne & Leonor García-Bayona & Michelle P. Christie & Jordan C. Evans & Allison J. Farrand & Katia Flo, 2024. "Distant relatives of a eukaryotic cell-specific toxin family evolved a complement-like mechanism to kill bacteria," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    2. Ming Tong & Jinghua Xu & Weixun Li & Kun Jiang & Yan Yang & Zhe Chen & Xuyao Jiao & Xiangfeng Meng & Mingyu Wang & Jie Hong & Hongan Long & Shuang-Jiang Liu & Bentley Lim & Xiang Gao, 2024. "A highly conserved SusCD transporter determines the import and species-specific antagonism of Bacteroides ubiquitin homologues," Nature Communications, Nature, vol. 15(1), pages 1-17, December.

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