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The architecture and stabilisation of flagellotropic tailed bacteriophages.

Authors :
Hardy JM
Dunstan RA
Grinter R
Belousoff MJ
Wang J
Pickard D
Venugopal H
Dougan G
Lithgow T
Coulibaly F
Source :
Nature communications [Nat Commun] 2020 Jul 27; Vol. 11 (1), pp. 3748. Date of Electronic Publication: 2020 Jul 27.
Publication Year :
2020

Abstract

Flagellotropic bacteriophages engage flagella to reach the bacterial surface as an effective means to increase the capture radius for predation. Structural details of these viruses are of great interest given the substantial drag forces and torques they face when moving down the spinning flagellum. We show that the main capsid and auxiliary proteins form two nested chainmails that ensure the integrity of the bacteriophage head. Core stabilising structures are conserved in herpesviruses suggesting their ancestral origin. The structure of the tail also reveals a robust yet pliable assembly. Hexameric rings of the tail-tube protein are braced by the N-terminus and a β-hairpin loop, and interconnected along the tail by the splayed β-hairpins. By contrast, we show that the β-hairpin has an inhibitory role in the tail-tube precursor, preventing uncontrolled self-assembly. Dyads of acidic residues inside the tail-tube present regularly-spaced motifs well suited to DNA translocation into bacteria through the tail.

Details

Language :
English
ISSN :
2041-1723
Volume :
11
Issue :
1
Database :
MEDLINE
Journal :
Nature communications
Publication Type :
Academic Journal
Accession number :
32719311
Full Text :
https://doi.org/10.1038/s41467-020-17505-w