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  • 1
    Publication Date: 2016-05-20
    Description: Several systems, including contractile tail bacteriophages, the type VI secretion system and R-type pyocins, use a multiprotein tubular apparatus to attach to and penetrate host cell membranes. This macromolecular machine resembles a stretched, coiled spring (or sheath) wound around a rigid tube with a spike-shaped protein at its tip. A baseplate structure, which is arguably the most complex part of this assembly, relays the contraction signal to the sheath. Here we present the atomic structure of the approximately 6-megadalton bacteriophage T4 baseplate in its pre- and post-host attachment states and explain the events that lead to sheath contraction in atomic detail. We establish the identity and function of a minimal set of components that is conserved in all contractile injection systems and show that the triggering mechanism is universally conserved.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taylor, Nicholas M I -- Prokhorov, Nikolai S -- Guerrero-Ferreira, Ricardo C -- Shneider, Mikhail M -- Browning, Christopher -- Goldie, Kenneth N -- Stahlberg, Henning -- Leiman, Petr G -- England -- Nature. 2016 May 18;533(7603):346-52. doi: 10.1038/nature17971.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ecole Polytechnique Federale de Lausanne (EPFL), BSP-415, 1015 Lausanne, Switzerland. ; Winogradsky Institute of Microbiology, Research Center of Biotechnology of the Russian Academy of Sciences, pr. 60-letiya Oktyabrya, 7 build. 2, 117312, Moscow, Russia. ; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Laboratory of Molecular Bioengineering, 16/10 Miklukho-Maklaya St., 117997 Moscow, Russia. ; Center for Cellular Imaging and NanoAnalytics (C-CINA), Biozentrum, University of Basel, Mattenstrasse 26, 4058 Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/27193680" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2011-06-15
    Description: 2D and 3D cryo-electron microscopy, together with adsorption kinetics assays of ϕCb13 and ϕCbK phage-infected Caulobacter crescentus, provides insight into the mechanisms of infection. ϕCb13 and ϕCbK actively interact with the flagellum and subsequently attach to receptors on the cell pole. We present evidence that the first interaction of the phage with the bacterial flagellum takes place through a filament on the phage head. This contact with the flagellum facilitates concentration of phage particles around the receptor (i.e., the pilus portals) on the bacterial cell surface, thereby increasing the likelihood of infection. Phage head filaments have not been well characterized and their function is described here. Phage head filaments may systematically underlie the initial interactions of phages with their hosts in other systems and possibly represent a widespread mechanism of efficient phage propagation.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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  • 3
    Publication Date: 2019
    Description: 〈p〉Contractile injection systems (bacteriophage tails, type VI secretions system, R-type pyocins, etc.) utilize a rigid tube/contractile sheath assembly for breaching the envelope of bacterial and eukaryotic cells. Among contractile injection systems, bacteriophages that infect Gram-positive bacteria represent the least understood members. Here, we describe the structure of 〈i〉Listeria〈/i〉 bacteriophage A511 tail in its pre- and post-host attachment states (extended and contracted, respectively) using cryo-electron microscopy, cryo-electron tomography, and X-ray crystallography. We show that the structure of the tube-baseplate complex of A511 is similar to that of phage T4, but the A511 baseplate is decorated with different receptor-binding proteins, which undergo a large structural transformation upon host attachment and switch the symmetry of the baseplate-tail fiber assembly from threefold to sixfold. For the first time under native conditions, we show that contraction of the phage tail sheath assembly starts at the baseplate and propagates through the sheath in a domino-like motion.〈/p〉
    Print ISSN: 0261-4189
    Electronic ISSN: 1460-2075
    Topics: Biology , Medicine
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  • 4
    Publication Date: 2019
    Description: 〈sec〉〈st〉Synopsis〈/st〉〈p〉〈textbox textbox-type="graphic"〉〈p〉〈inline-fig〉〈/inline-fig〉〈/p〉〈/textbox〉〈/p〉 〈p〉The attachment and host envelope penetration mechanism of bacteriophages that employ a rigid tube/contractile sheath complex for infection of Gram-positive bacteria is poorly understood. This study describes the structure of the 〈i〉Listeria〈/i〉 phage A511 contractile tail in the pre- and post-host attachment state.〈/p〉 〈p〉 〈l type="unord"〉〈li〉〈p〉The A511 baseplate-tail fiber complex undergoes a massive conformational change and switches from threefold to sixfold symmetry upon attachment to the host cell.〈/p〉〈/li〉 〈li〉〈p〉The distal tail fiber protein gp108 attaches to the host cell wall before the sheath contracts.〈/p〉〈/li〉 〈li〉〈p〉The proximal part of the tail fiber carries two pyramids that are formed by gp106 trimers.〈/p〉〈/li〉 〈li〉〈p〉The gp106 pyramids reorient to point toward the cell surface, change their conformation to protrude attachment domain, and bind to the cell wall.〈/p〉〈/li〉 〈li〉〈p〉Contraction of the phage tail sheath assembly starts at the baseplate and propagates through the sheath in a wave-like motion.〈/p〉〈/li〉〈/l〉 〈/p〉〈/sec〉
    Print ISSN: 0261-4189
    Electronic ISSN: 1460-2075
    Topics: Biology , Medicine
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