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CryoEM structure and assembly mechanism of a bacterial virus genome gatekeeper

Orlov, I., Roche, S., Brasilès, S., Lukoyanova, N., Vaney, M.-C., Tavares, P. and Orlova, E. V. (2022) CryoEM structure and assembly mechanism of a bacterial virus genome gatekeeper. Nature Communications, 13, 7283. (doi: 10.1038/s41467-022-34999-8) (PMID:36435855) (PMCID:PMC9701221)

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Abstract

Numerous viruses package their dsDNA genome into preformed capsids through a portal gatekeeper that is subsequently closed. We report the structure of the DNA gatekeeper complex of bacteriophage SPP1 (gp612gp1512gp166) in the post-DNA packaging state at 2.7 Å resolution obtained by single particle cryo-electron microscopy. Comparison of the native SPP1 complex with assembly-naïve structures of individual components uncovered the complex program of conformational changes leading to its assembly. After DNA packaging, gp15 binds via its C-terminus to the gp6 oligomer positioning gp15 subunits for oligomerization. Gp15 refolds its inner loops creating an intersubunit β-barrel that establishes different types of contacts with six gp16 subunits. Gp16 binding and oligomerization is accompanied by folding of helices that close the portal channel to keep the viral genome inside the capsid. This mechanism of assembly has broad functional and evolutionary implications for viruses of the prokaryotic tailed viruses-herpesviruses lineage.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Orlov, Dr Igor
Authors: Orlov, I., Roche, S., Brasilès, S., Lukoyanova, N., Vaney, M.-C., Tavares, P., and Orlova, E. V.
College/School:College of Medical Veterinary and Life Sciences > School of Infection & Immunity > Centre for Virus Research
Journal Name:Nature Communications
Publisher:Nature Research
ISSN:2041-1723
ISSN (Online):2041-1723
Copyright Holders:Copyright © 2022 The Authors
First Published:First published in Nature Communications 13: 7283
Publisher Policy:Reproduced under a Creative Commons License

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