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Diverse type VI secretion phospholipases are functionally plastic antibacterial effectors

Author

Listed:
  • Alistair B. Russell

    (University of Washington)

  • Michele LeRoux

    (University of Washington
    Molecular and Cellular Biology Program, University of Washington)

  • Krisztina Hathazi

    (Umeå University, SE-90187 Umeå, Sweden
    The Laboratory for Molecular Infection Medicine Sweden (MIMS), Umeå University, SE-90187 Umeå, Sweden)

  • Danielle M. Agnello

    (University of Washington)

  • Takahiko Ishikawa

    (Umeå University, SE-90187 Umeå, Sweden
    The Laboratory for Molecular Infection Medicine Sweden (MIMS), Umeå University, SE-90187 Umeå, Sweden)

  • Paul A. Wiggins

    (University of Washington
    University of Washington)

  • Sun Nyunt Wai

    (Umeå University, SE-90187 Umeå, Sweden
    The Laboratory for Molecular Infection Medicine Sweden (MIMS), Umeå University, SE-90187 Umeå, Sweden)

  • Joseph D. Mougous

    (University of Washington
    Molecular and Cellular Biology Program, University of Washington)

Abstract

A functionally diverse superfamily of bacterial phospholipase enzymes that mediate antagonisitc interactions as effectors of the type VI secretion system is uncovered; these enzymes degrade the bacterial membrane, representing a novel mechanism of bacterial competition.

Suggested Citation

  • Alistair B. Russell & Michele LeRoux & Krisztina Hathazi & Danielle M. Agnello & Takahiko Ishikawa & Paul A. Wiggins & Sun Nyunt Wai & Joseph D. Mougous, 2013. "Diverse type VI secretion phospholipases are functionally plastic antibacterial effectors," Nature, Nature, vol. 496(7446), pages 508-512, April.
    • Handle: RePEc:nat:nature:v:496:y:2013:i:7446:d:10.1038_nature12074
    DOI: 10.1038/nature12074
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    Cited by:

    1. Po-Yin Chen & Yung-Chih Chen & Po-Pang Chen & Kuan-Ting Lin & Karen Sargsyan & Chao-Ping Hsu & Wei-Le Wang & Kuo-Chiang Hsia & See-Yeun Ting, 2024. "A whole-cell platform for discovering synthetic cell adhesion molecules in bacteria," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    2. Steven J. Jensen & Bonnie J. Cuthbert & Fernando Garza-Sánchez & Colette C. Helou & Rodger Miranda & Celia W. Goulding & Christopher S. Hayes, 2024. "Advanced glycation end-product crosslinking activates a type VI secretion system phospholipase effector protein," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    3. Katarzyna Kanarek & Chaya Mushka Fridman & Eran Bosis & Dor Salomon, 2023. "The RIX domain defines a class of polymorphic T6SS effectors and secreted adaptors," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    4. Xiaoyun Yang & Zongqiang Li & Liang Zhao & Zhun She & Zengqiang Gao & Sen-Fang Sui & Yuhui Dong & Yanhua Li, 2022. "Structural insights into PA3488-mediated inactivation of Pseudomonas aeruginosa PldA," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    5. Stephen R. Garrett & Nicole Mietrach & Justin Deme & Alina Bitzer & Yaping Yang & Fatima R. Ulhuq & Dorothee Kretschmer & Simon Heilbronner & Terry K. Smith & Susan M. Lea & Tracy Palmer, 2023. "A type VII-secreted lipase toxin with reverse domain arrangement," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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