The architecture and stabilisation of flagellotropic tailed bacteriophages.
Joshua M. Hardy,Rhys A. Dunstan,Rhys Grinter,Matthew J. Belousoff,Jiawei Wang,Derek Pickard,Hariprasad Venugopal,Gordon Dougan,Gordon Dougan,Trevor Lithgow,Fasséli Coulibaly +10 more
TLDR
How two nested sets of chainmail stabilise the viral head and a beta-hairpin regulates the formation of the robust yet pliable tail, characteristic of siphoviruses is shown.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.read more
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Architecture of the flexible tail tube of bacteriophage SPP1.
Maximilian Zinke,Katrin A. A. Sachowsky,Carl Öster,Sophie Zinn-Justin,Raimond B. G. Ravelli,Gunnar F. Schröder,Gunnar F. Schröder,Michael Habeck,Adam Lange +8 more
TL;DR: The atomic structure of the tail tube of phage SPP1 is presented and it is shown that the tailTube protein gp17.1 organizes into hexameric rings that are stacked by flexible linker domains and, thus, form a hollow flexible tube with a negatively charged lumen suitable for the transport of DNA.
Journal ArticleDOI
Major tail proteins of bacteriophages of the order Caudovirales
Adam Lange,Maximilian Zinke +1 more
TL;DR: In this article , the structural elements of major tail proteins of Caudovirales are summarized, and the authors discuss how different amounts of tail tube flexibility confer heterogeneity within cryo-EM maps and thus limit high-resolution reconstructions.
Journal ArticleDOI
Mechanistic Insights into the Capsule-Targeting Depolymerase from a Klebsiella pneumoniae Bacteriophage.
Rhys A. Dunstan,Rebecca S. Bamert,Matthew J Belousoff,Francesca L. Short,Francesca L. Short,Francesca L. Short,Christopher K. Barlow,Derek Pickard,Jonathan J. Wilksch,Ralf B. Schittenhelm,Richard A. Strugnell,Gordon Dougan,Trevor Lithgow +12 more
TL;DR: In this article, the first structure of a depolymerase that targets the clinically relevant K2 capsule was determined and its putative active site was identified, comprising clustered negatively charged residues that could facilitate the hydrolysis of target polysaccharides.
Journal ArticleDOI
Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins.
TL;DR: Because of their unique abilities to bind virus surfaces noncovalently, decoration proteins are increasingly exploited for technology, with uses including phage display, viral functionalization, vaccination, and improved nanoparticle design for imaging and drug delivery.
Journal ArticleDOI
Structural basis of bacteriophage lambda capsid maturation.
TL;DR: In this article , the authors determined the Cryo-Electron microscopy structures of the bacteriophage lambda procapsid and mature capsid at 3.88 Å and 3.76 Å resolution, respectively.
References
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