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Structure of an F-type phage tail-like bacteriocin from Listeria monocytogenes

Author

Listed:
  • Zhiwei Gu

    (Tsinghua University)

  • Xiaofei Ge

    (City University of Macau)

  • Jiawei Wang

    (Tsinghua University)

Abstract

F-type phage tail-like bacteriocins (PTLBs) are high-molecular-weight protein complexes exhibiting bactericidal activity and share evolutionary similarities with the tails of non-contractile siphoviruses. In this study, we present the atomic structure of monocin, a genetically engineered F-type PTLB from Listeria monocytogenes. Our detailed atomic-level analysis, excluding two chaperone proteins, provides crucial insights into the molecular architecture of F-type PTLBs. The core structure of monocin resembles TP901-1-like phage tails, featuring three side fibers with receptor-binding domains that connect to the baseplate for host adhesion. Based on these findings, we propose a potential mechanism by which F-type PTLBs induce cell death, offering a foundation for developing targeted antibacterial therapies.

Suggested Citation

  • Zhiwei Gu & Xiaofei Ge & Jiawei Wang, 2025. "Structure of an F-type phage tail-like bacteriocin from Listeria monocytogenes," Nature Communications, Nature, vol. 16(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-57075-3
    DOI: 10.1038/s41467-025-57075-3
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