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  1. Article ; Online: Stretching the arms of the type VI secretion sheath protein.

    Leiman, Petr G

    EMBO reports

    2018  Volume 19, Issue 2, Page(s) 191–193

    MeSH term(s) Bacterial Proteins ; Bacterial Secretion Systems ; Type VI Secretion Systems
    Chemical Substances Bacterial Proteins ; Bacterial Secretion Systems ; Type VI Secretion Systems
    Language English
    Publishing date 2018-01-22
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 2020896-0
    ISSN 1469-3178 ; 1469-221X
    ISSN (online) 1469-3178
    ISSN 1469-221X
    DOI 10.15252/embr.201745627
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5433: Show issues Location:
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  2. Article: Function of the bacteriophage P2 baseplate central spike Apex domain in the infection process.

    Miller, John-Mark / Knyazhanskaya, Ekaterina S / Buth, Sergii A / Prokhorov, Nikolai S / Leiman, Petr G

    bioRxiv : the preprint server for biology

    2023  

    Abstract: The contractile tail of bacteriophage P2 functions to drive the tail tube across the outer membrane of its host bacterium, a prerequisite event for subsequent translocation of phage genomic DNA into the host cell. The tube is equipped with a spike-shaped ...

    Abstract The contractile tail of bacteriophage P2 functions to drive the tail tube across the outer membrane of its host bacterium, a prerequisite event for subsequent translocation of phage genomic DNA into the host cell. The tube is equipped with a spike-shaped protein (product of P2 gene
    Language English
    Publishing date 2023-02-25
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.02.25.529910
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Editorial overview: Virus structure and expression.

    Taylor, Nicholas M I / Leiman, Petr G

    Current opinion in virology

    2020  Volume 45, Page(s) iii–v

    MeSH term(s) Humans ; Viral Structures ; Virus Diseases/virology ; Viruses/chemistry ; Viruses/genetics
    Language English
    Publishing date 2020-12-14
    Publishing country Netherlands
    Document type Editorial
    ZDB-ID 2611378-8
    ISSN 1879-6265 ; 1879-6257
    ISSN (online) 1879-6265
    ISSN 1879-6257
    DOI 10.1016/j.coviro.2020.11.005
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  4. Article ; Online: Reprogramming bacteriophage host range: design principles and strategies for engineering receptor binding proteins.

    Dunne, Matthew / Prokhorov, Nikolai S / Loessner, Martin J / Leiman, Petr G

    Current opinion in biotechnology

    2021  Volume 68, Page(s) 272–281

    Abstract: Bacteriophages (phages) use specialized tail machinery to deliver proteins and genetic material into a bacterial cell during infection. Attached at the distal ends of their tails are receptor binding proteins (RBPs) that recognize specific molecules ... ...

    Abstract Bacteriophages (phages) use specialized tail machinery to deliver proteins and genetic material into a bacterial cell during infection. Attached at the distal ends of their tails are receptor binding proteins (RBPs) that recognize specific molecules exposed on host bacteria surfaces. Since the therapeutic capacity of naturally occurring phages is often limited by narrow host ranges, there is significant interest in expanding their host range via directed evolution or structure-guided engineering of their RBPs. Here, we describe the design principles of different RBP engineering platforms and draw attention to the mechanisms linking RBP binding and the correct spatial and temporal attachment of the phage to the bacterial surface. A deeper understanding of these mechanisms will directly benefit future engineering of more effective phage-based therapeutics.
    MeSH term(s) Bacteriophages/genetics ; Carrier Proteins ; Host Specificity ; Protein Binding ; Protein Engineering
    Chemical Substances Carrier Proteins
    Language English
    Publishing date 2021-03-18
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1052045-4
    ISSN 1879-0429 ; 0958-1669
    ISSN (online) 1879-0429
    ISSN 0958-1669
    DOI 10.1016/j.copbio.2021.02.006
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3071: Show issues Location:
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  5. Article ; Online: An extensive disulfide bond network prevents tail contraction in Agrobacterium tumefaciens phage Milano.

    Sonani, Ravi R / Palmer, Lee K / Esteves, Nathaniel C / Horton, Abigail A / Sebastian, Amanda L / Kelly, Rebecca J / Wang, Fengbin / Kreutzberger, Mark A B / Russell, William K / Leiman, Petr G / Scharf, Birgit E / Egelman, Edward H

    Nature communications

    2024  Volume 15, Issue 1, Page(s) 756

    Abstract: A contractile sheath and rigid tube assembly is a widespread apparatus used by bacteriophages, tailocins, and the bacterial type VI secretion system to penetrate cell membranes. In this mechanism, contraction of an external sheath powers the motion of an ...

    Abstract A contractile sheath and rigid tube assembly is a widespread apparatus used by bacteriophages, tailocins, and the bacterial type VI secretion system to penetrate cell membranes. In this mechanism, contraction of an external sheath powers the motion of an inner tube through the membrane. The structure, energetics, and mechanism of the machinery imply rigidity and straightness. The contractile tail of Agrobacterium tumefaciens bacteriophage Milano is flexible and bent to varying degrees, which sets it apart from other contractile tail-like systems. Here, we report structures of the Milano tail including the sheath-tube complex, baseplate, and putative receptor-binding proteins. The flexible-to-rigid transformation of the Milano tail upon contraction can be explained by unique electrostatic properties of the tail tube and sheath. All components of the Milano tail, including sheath subunits, are crosslinked by disulfides, some of which must be reduced for contraction to occur. The putative receptor-binding complex of Milano contains a tailspike, a tail fiber, and at least two small proteins that form a garland around the distal ends of the tailspikes and tail fibers. Despite being flagellotropic, Milano lacks thread-like tail filaments that can wrap around the flagellum, and is thus likely to employ a different binding mechanism.
    MeSH term(s) Bacteriophages/genetics ; Agrobacterium tumefaciens/genetics ; Type VI Secretion Systems/metabolism ; Cell Membrane/metabolism
    Chemical Substances Type VI Secretion Systems
    Language English
    Publishing date 2024-01-26
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-024-44959-z
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Modeling the Architecture of Depolymerase-Containing Receptor Binding Proteins in

    Latka, Agnieszka / Leiman, Petr G / Drulis-Kawa, Zuzanna / Briers, Yves

    Frontiers in microbiology

    2019  Volume 10, Page(s) 2649

    Abstract: Klebsiella ... ...

    Abstract Klebsiella pneumoniae
    Language English
    Publishing date 2019-11-15
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2587354-4
    ISSN 1664-302X
    ISSN 1664-302X
    DOI 10.3389/fmicb.2019.02649
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  7. Article ; Online: Quantitative description of a contractile macromolecular machine.

    Fraser, Alec / Prokhorov, Nikolai S / Jiao, Fang / Pettitt, B Montgomery / Scheuring, Simon / Leiman, Petr G

    Science advances

    2021  Volume 7, Issue 24

    Abstract: Contractile injection systems (CISs) [type VI secretion system (T6SS), phage tails, and tailocins] use a contractile sheath-rigid tube machinery to breach cell walls and lipid membranes. The structures of the pre- and postcontraction states of several ... ...

    Abstract Contractile injection systems (CISs) [type VI secretion system (T6SS), phage tails, and tailocins] use a contractile sheath-rigid tube machinery to breach cell walls and lipid membranes. The structures of the pre- and postcontraction states of several CISs are known, but the mechanism of contraction remains poorly understood. Combining structural information of the end states of the 12-megadalton R-type pyocin sheath-tube complex with thermodynamic and force spectroscopy analyses and an original modeling procedure, we describe the mechanism of pyocin contraction. We show that this nanomachine has an activation energy of 160 kilocalories/mole (kcal/mol), and it releases 2160 kcal/mol of heat and develops a force greater than 500 piconewtons. Our combined approach provides a quantitative and experimental description of the membrane penetration process by a CIS.
    Language English
    Publishing date 2021-06-11
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2810933-8
    ISSN 2375-2548 ; 2375-2548
    ISSN (online) 2375-2548
    ISSN 2375-2548
    DOI 10.1126/sciadv.abf9601
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  8. Article ; Online ; Conference proceedings: Introduction to “Viruses of Microbes III” special section of Virology.

    Leiman, Petr G / Molineux, Ian J

    Virology

    2015  Volume 477, Page(s) 99

    MeSH term(s) Biodiversity ; Virology/trends ; Virus Physiological Phenomena ; Viruses/classification ; Viruses/genetics ; Viruses/isolation & purification
    Language English
    Publishing date 2015-03
    Publishing country United States
    Document type Congresses ; Editorial
    ZDB-ID 200425-2
    ISSN 1096-0341 ; 0042-6822
    ISSN (online) 1096-0341
    ISSN 0042-6822
    DOI 10.1016/j.virol.2015.01.001
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    In stock of ZB MED Cologne/Königswinter

    Ud II Zs.172: Show issues Location:
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  9. Article ; Online: Structural basis of template strand deoxyuridine promoter recognition by a viral RNA polymerase.

    Fraser, Alec / Sokolova, Maria L / Drobysheva, Arina V / Gordeeva, Julia V / Borukhov, Sergei / Jumper, John / Severinov, Konstantin V / Leiman, Petr G

    Nature communications

    2022  Volume 13, Issue 1, Page(s) 3526

    Abstract: Recognition of promoters in bacterial RNA polymerases (RNAPs) is controlled by sigma subunits. The key sequence motif recognized by the sigma, the -10 promoter element, is located in the non-template strand of the double-stranded DNA molecule ~10 ... ...

    Abstract Recognition of promoters in bacterial RNA polymerases (RNAPs) is controlled by sigma subunits. The key sequence motif recognized by the sigma, the -10 promoter element, is located in the non-template strand of the double-stranded DNA molecule ~10 nucleotides upstream of the transcription start site. Here, we explain the mechanism by which the phage AR9 non-virion RNAP (nvRNAP), a bacterial RNAP homolog, recognizes the -10 element of its deoxyuridine-containing promoter in the template strand. The AR9 sigma-like subunit, the nvRNAP enzyme core, and the template strand together form two nucleotide base-accepting pockets whose shapes dictate the requirement for the conserved deoxyuridines. A single amino acid substitution in the AR9 sigma-like subunit allows one of these pockets to accept a thymine thus expanding the promoter consensus. Our work demonstrates the extent to which viruses can evolve host-derived multisubunit enzymes to make transcription of their own genes independent of the host.
    MeSH term(s) DNA-Directed RNA Polymerases/metabolism ; Deoxyuridine ; Promoter Regions, Genetic/genetics ; RNA, Viral ; Sigma Factor/metabolism ; Transcription, Genetic ; Viral Replicase Complex Proteins
    Chemical Substances RNA, Viral ; Sigma Factor ; Viral Replicase Complex Proteins ; DNA-Directed RNA Polymerases (EC 2.7.7.6) ; Deoxyuridine (W78I7AY22C)
    Language English
    Publishing date 2022-06-20
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-022-31214-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Structure and Function of the T4 Spackle Protein Gp61.3.

    Kanamaru, Shuji / Uchida, Kazuya / Nemoto, Mai / Fraser, Alec / Arisaka, Fumio / Leiman, Petr G

    Viruses

    2020  Volume 12, Issue 10

    Abstract: The bacteriophage T4 genome contains two genes that code for proteins with lysozyme activity- ...

    Abstract The bacteriophage T4 genome contains two genes that code for proteins with lysozyme activity-
    MeSH term(s) Bacteriophage T4/enzymology ; Bacteriophage T4/genetics ; Crystallography, X-Ray ; Escherichia coli/virology ; Genome, Viral/genetics ; Muramidase/antagonists & inhibitors ; Protein Conformation ; Viral Proteins/genetics ; Viral Proteins/metabolism
    Chemical Substances Viral Proteins ; spackle protein, bacteriophage T4 ; Muramidase (EC 3.2.1.17)
    Language English
    Publishing date 2020-09-24
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v12101070
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