Visualizing a complete Siphoviridae member by single-particle electron microscopy: the structure of lactococcal phage TP901-1

TY - JOUR

T1 - Visualizing a complete Siphoviridae member by single-particle electron microscopy

T2 - the structure of lactococcal phage TP901-1

AU - Bebeacua, Cecilia

AU - Lai, Livia

AU - Vegge, Christina Skovgaard

AU - Brøndsted, Lone

AU - van Heel, Marin

AU - Veesler, David

AU - Cambillau, Christian

PY - 2013/1

Y1 - 2013/1

N2 - 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.

AB - 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.

KW - Bacteriophages

KW - Lactococcus lactis

KW - Microscopy, Electron

KW - Models, Biological

KW - Models, Molecular

KW - Siphoviridae

U2 - 10.1128/JVI.02836-12

DO - 10.1128/JVI.02836-12

M3 - Journal article

C2 - 23135714

SN - 0022-538X

VL - 87

SP - 1061

EP - 1068

JO - Journal of Virology

JF - Journal of Virology

IS - 2

ER -