Visualizing a Complete Siphoviridae Member by Single-Particle Electron Microscopy: the Structure of Lactococcal Phage TP901-1

被引:55
作者
Bebeacua, Cecilia [1 ,3 ,4 ,5 ]
Lai, Livia [1 ]
Vegge, Christina Skovgaard [2 ]
Brondsted, Lone [2 ]
van Heel, Marin [1 ]
Veesler, David [3 ,4 ,5 ]
Cambillau, Christian [3 ,4 ,5 ]
机构
[1] Univ London Imperial Coll Sci Technol & Med, Div Biol Sci, London, England
[2] Univ Copenhagen, Dept Vet Dis Biol, Frederiksberg, Denmark
[3] CNRS, UMR 6098, F-75700 Paris, France
[4] Univ Aix Marseille 1, F-13331 Marseille 3, France
[5] Univ Aix Marseille 2, F-13284 Marseille 07, France
基金
英国生物技术与生命科学研究理事会;
关键词
RECEPTOR-BINDING PROTEIN; SUBSP LACTIS C2; BACTERIOPHAGE SPP1; MEMBRANE-PROTEIN; DNA EJECTION; 3-DIMENSIONAL STRUCTURE; CRYSTAL-STRUCTURE; PORTAL PROTEIN; CELL-SURFACE; IN-VITRO;
D O I
10.1128/JVI.02836-12
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
引用
收藏
页码:1061 / 1068
页数:8
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