Journal: J Virol / Year: 2013 Title: Structure, adsorption to host, and infection mechanism of virulent lactococcal phage p2. Authors: Cecilia Bebeacua / Denise Tremblay / Carine Farenc / Marie-Pierre Chapot-Chartier / Irina Sadovskaya / Marin van Heel / David Veesler / Sylvain Moineau / Christian Cambillau / Abstract: Lactococcal siphophages from the 936 and P335 groups infect the Gram-positive bacterium Lactococcus lactis using receptor binding proteins (RBPs) attached to their baseplate, a large multiprotein ...Lactococcal siphophages from the 936 and P335 groups infect the Gram-positive bacterium Lactococcus lactis using receptor binding proteins (RBPs) attached to their baseplate, a large multiprotein complex at the distal part of the tail. We have previously reported the crystal and electron microscopy (EM) structures of the baseplates of phages p2 (936 group) and TP901-1 (P335 group) as well as the full EM structure of the TP901-1 virion. Here, we report the complete EM structure of siphophage p2, including its capsid, connector complex, tail, and baseplate. Furthermore, we show that the p2 tail is characterized by the presence of protruding decorations, which are related to adhesins and are likely contributed by the major tail protein C-terminal domains. This feature is reminiscent of the tail of Escherichia coli phage λ and Bacillus subtilis phage SPP1 and might point to a common mechanism for establishing initial interactions with their bacterial hosts. Comparative analyses showed that the architecture of the phage p2 baseplate differs largely from that of lactococcal phage TP901-1. We quantified the interaction of its RBP with the saccharidic receptor and determined that specificity is due to lower k(off) values of the RBP/saccharidic dissociation. Taken together, these results suggest that the infection of L. lactis strains by phage p2 is a multistep process that involves reversible attachment, followed by baseplate activation, specific attachment of the RBPs to the saccharidic receptor, and DNA ejection.
History
Deposition
Sep 11, 2013
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Header (metadata) release
Sep 25, 2013
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Map release
Sep 25, 2013
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Update
Apr 16, 2014
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Current status
Apr 16, 2014
Processing site: PDBe / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Shell ID: 1 / Name: T7 / Diameter: 660 Å / T number (triangulation number): 7
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Experimental details
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Structure determination
Processing
single particle reconstruction
Aggregation state
particle
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Sample preparation
Buffer
pH: 7.5 / Details: 50 mM Tris-HCl, 100 mM NaCl, 8 mM MgSO4
Grid
Details: Quantifoil grids
Vitrification
Cryogen name: NONE / Instrument: OTHER
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Electron microscopy
Microscope
FEI/PHILIPS CM200T
Alignment procedure
Legacy - Astigmatism: Objective lens astigmatism was corrected at 100,000 times magnification.
Date
Jul 1, 2009
Image recording
Category: CCD / Film or detector model: GENERIC TVIPS (4k x 4k) / Digitization - Sampling interval: 4.64 µm / Number real images: 1000 / Average electron dose: 10 e/Å2
Electron beam
Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
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