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Visualizing a Complete Siphoviridae Member by Single-Particle Electron Microscopy: the Structure of Lactococcal Phage TP901-1
Authors:Cecilia Bebeacua  Livia Lai  Christina Skovgaard Vegge  Lone Br?ndsted  Marin van Heel  David Veesler  Christian Cambillau
Institution:aDivision of Biological Sciences, Imperial College London, South Kensington Campus, London, United Kingdom;bDepartment of Veterinary Disease Biology, University of Copenhagen, Frederiksberg, Denmark;cArchitecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS and Universités Aix-Marseille I and II, Campus de Luminy, France
Abstract:Tailed phages are genome delivery machines exhibiting unequaled efficiency acquired over more than 3 billion years of evolution. Siphophages from the P335 and 936 families infect the Gram-positive bacterium Lactococcus lactis using receptor-binding proteins anchored to the host adsorption apparatus (baseplate). Crystallographic and electron microscopy (EM) studies have shed light on the distinct adsorption strategies used by phages of these two families, suggesting that they might also rely on different infection mechanisms. Here, we report electron microscopy reconstructions of the whole phage TP901-1 (P335 species) and propose a composite EM model of this gigantic molecular machine. Our results suggest conservation of structural proteins among tailed phages and add to the growing body of evidence pointing to a common evolutionary origin for these virions. Finally, we propose that host adsorption apparatus architectures have evolved in correlation with the nature of the receptors used during infection.
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