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

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-...

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Main Authors: Zhiwei Gu, Xiaofei Ge, Jiawei Wang
Format: Article
Language:English
Published: Nature Portfolio 2025-02-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-025-57075-3
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author Zhiwei Gu
Xiaofei Ge
Jiawei Wang
author_facet Zhiwei Gu
Xiaofei Ge
Jiawei Wang
author_sort Zhiwei Gu
collection DOAJ
description 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.
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issn 2041-1723
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publishDate 2025-02-01
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series Nature Communications
spelling doaj-art-68a8bb84fc344736aeb545d41336e4bf2025-08-20T03:10:50ZengNature PortfolioNature Communications2041-17232025-02-011611910.1038/s41467-025-57075-3Structure of an F-type phage tail-like bacteriocin from Listeria monocytogenesZhiwei Gu0Xiaofei Ge1Jiawei Wang2State Key Laboratory of Membrane Biology, Beijing Frontier Research Center for Biological Structure, School of Life Sciences, Tsinghua UniversityHealth and Wellness, City University of MacauState Key Laboratory of Membrane Biology, Beijing Frontier Research Center for Biological Structure, School of Life Sciences, Tsinghua UniversityAbstract 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.https://doi.org/10.1038/s41467-025-57075-3
spellingShingle Zhiwei Gu
Xiaofei Ge
Jiawei Wang
Structure of an F-type phage tail-like bacteriocin from Listeria monocytogenes
Nature Communications
title Structure of an F-type phage tail-like bacteriocin from Listeria monocytogenes
title_full Structure of an F-type phage tail-like bacteriocin from Listeria monocytogenes
title_fullStr Structure of an F-type phage tail-like bacteriocin from Listeria monocytogenes
title_full_unstemmed Structure of an F-type phage tail-like bacteriocin from Listeria monocytogenes
title_short Structure of an F-type phage tail-like bacteriocin from Listeria monocytogenes
title_sort structure of an f type phage tail like bacteriocin from listeria monocytogenes
url https://doi.org/10.1038/s41467-025-57075-3
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AT jiaweiwang structureofanftypephagetaillikebacteriocinfromlisteriamonocytogenes