Details

Autor(en) / Beteiligte

• Guerrero‐Ferreira, Ricardo C
• Hupfeld, Mario
• Nazarov, Sergey
• Taylor, Nicholas MI
• Shneider, Mikhail M
• Obbineni, Jagan M
• Loessner, Martin J
• Ishikawa, Takashi
• Klumpp, Jochen
• Leiman, Petr G

Titel

Structure and transformation of bacteriophage A511 baseplate and tail upon infection of Listeria cells

Ist Teil von

• The EMBO journal, 2019-02, Vol.38 (3), p.n/a

Ort / Verlag

England: Blackwell Publishing Ltd

Erscheinungsjahr

2019

Quelle

Access via Wiley Online Library

Beschreibungen/Notizen

• Contractile injection systems (bacteriophage tails, type VI secretions system, R‐type pyocins, etc.) utilize a rigid tube/contractile sheath assembly for breaching the envelope of bacterial and eukaryotic cells. Among contractile injection systems, bacteriophages that infect Gram‐positive bacteria represent the least understood members. Here, we describe the structure of Listeria bacteriophage A511 tail in its pre‐ and post‐host attachment states (extended and contracted, respectively) using cryo‐electron microscopy, cryo‐electron tomography, and X‐ray crystallography. We show that the structure of the tube‐baseplate complex of A511 is similar to that of phage T4, but the A511 baseplate is decorated with different receptor‐binding proteins, which undergo a large structural transformation upon host attachment and switch the symmetry of the baseplate‐tail fiber assembly from threefold to sixfold. For the first time under native conditions, we show that contraction of the phage tail sheath assembly starts at the baseplate and propagates through the sheath in a domino‐like motion. Synopsis The attachment and host envelope penetration mechanism of bacteriophages that employ a rigid tube/contractile sheath complex for infection of Gram‐positive bacteria is poorly understood. This study describes the structure of the Listeria phage A511 contractile tail in the pre‐ and post‐host attachment state. The A511 baseplate‐tail fiber complex undergoes a massive conformational change and switches from threefold to sixfold symmetry upon attachment to the host cell. The distal tail fiber protein gp108 attaches to the host cell wall before the sheath contracts. The proximal part of the tail fiber carries two pyramids that are formed by gp106 trimers. The gp106 pyramids reorient to point toward the cell surface, change their conformation to protrude attachment domain, and bind to the cell wall. Contraction of the phage tail sheath assembly starts at the baseplate and propagates through the sheath in a wave‐like motion. A combination of cryo‐electron microscopy, cryo‐electron tomography and X‐ray crystallography reveals the structure of the Listeria bacteriophage A511 contractile tail in its pre‐ and post‐host attachment states.