Visualizing a complete Siphoviridae member by single-particle electron microscopy: the structure of lactococcal phage TP901-1
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Visualizing a complete Siphoviridae member by single-particle electron microscopy : the structure of lactococcal phage TP901-1. / Bebeacua, Cecilia; Lai, Livia; Vegge, Christina Skovgaard; Brøndsted, Lone; van Heel, Marin; Veesler, David; Cambillau, Christian.
I: Journal of Virology, Bind 87, Nr. 2, 2013, s. 1061-1068.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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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
Y1 - 2013
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
VL - 87
SP - 1061
EP - 1068
JO - Journal of Virology
JF - Journal of Virology
SN - 0022-538X
IS - 2
ER -
ID: 44533444