CryoEM Investigation of Three-Dimentional Structure of the Stx-Converting Bacteriophage ϕ24B

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A modified method for culturing, concentrating, and purifying phage ϕ24B preparations was developed. In particular, a new lysogenic phage-producing strain lacking flagella was used, induction conditions were optimized, and purification in a sucrose gradient and concentration by deposition on a Freon 113 cushion were used. Using this method, a preparation of the Stx-converting bacteriophage ϕ24B was obtained, which was suitable for direct analysis by the cryoEM method. Based on cryoEM data for this phage, the first primary three-dimensional reconstruction of its virions was performed. The structure of the phage ϕ24B tail is described. It was shown that the adsorption apparatus of this virus is represented by six thin lateral fibrils and an axial fibril located at the end of the tail. This arrangement of the tail structure is consistent with the previously proposed hypothesis based on analysis of the receptor binding proteins (RBPs) of this bacteriophage.

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作者简介

A. Kuznetsov

Research Center of Biotechnology, Russian Academy of Sciences

编辑信件的主要联系方式.
Email: alexbluesking@gmail.com
俄罗斯联邦, Moscow

A. Moiseenko

Lomonosov Moscow State University

Email: alexbluesking@gmail.com
俄罗斯联邦, Moscow

E. Kulikov

Research Center of Biotechnology, Russian Academy of Sciences

Email: alexbluesking@gmail.com
俄罗斯联邦, Moscow

A. Letarov

Research Center of Biotechnology, Russian Academy of Sciences; Lomonosov Moscow State University

Email: alexbluesking@gmail.com
俄罗斯联邦, Moscow; Moscow

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2. Fig. 1. Structural features of bacteriophage ϕ24B: a - SEM image of virions; b - three-dimensional reconstruction of the whole virion; c - three-dimensional reconstruction of the tail (the colour gradient from red to blue reflects the distance from the central axis of the tail)

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