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The architecture and stabilisation of flagellotropic tailed bacteriophages
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....
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7385642/ https://www.ncbi.nlm.nih.gov/pubmed/32719311 http://dx.doi.org/10.1038/s41467-020-17505-w |
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author | Hardy, Joshua M. Dunstan, Rhys A. Grinter, Rhys Belousoff, Matthew J. Wang, Jiawei Pickard, Derek Venugopal, Hariprasad Dougan, Gordon Lithgow, Trevor Coulibaly, Fasséli |
author_facet | Hardy, Joshua M. Dunstan, Rhys A. Grinter, Rhys Belousoff, Matthew J. Wang, Jiawei Pickard, Derek Venugopal, Hariprasad Dougan, Gordon Lithgow, Trevor Coulibaly, Fasséli |
author_sort | Hardy, Joshua M. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-7385642 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-73856422020-08-12 The architecture and stabilisation of flagellotropic tailed bacteriophages Hardy, Joshua M. Dunstan, Rhys A. Grinter, Rhys Belousoff, Matthew J. Wang, Jiawei Pickard, Derek Venugopal, Hariprasad Dougan, Gordon Lithgow, Trevor Coulibaly, Fasséli Nat Commun Article 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. Nature Publishing Group UK 2020-07-27 /pmc/articles/PMC7385642/ /pubmed/32719311 http://dx.doi.org/10.1038/s41467-020-17505-w Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Hardy, Joshua M. Dunstan, Rhys A. Grinter, Rhys Belousoff, Matthew J. Wang, Jiawei Pickard, Derek Venugopal, Hariprasad Dougan, Gordon Lithgow, Trevor Coulibaly, Fasséli The architecture and stabilisation of flagellotropic tailed bacteriophages |
title | The architecture and stabilisation of flagellotropic tailed bacteriophages |
title_full | The architecture and stabilisation of flagellotropic tailed bacteriophages |
title_fullStr | The architecture and stabilisation of flagellotropic tailed bacteriophages |
title_full_unstemmed | The architecture and stabilisation of flagellotropic tailed bacteriophages |
title_short | The architecture and stabilisation of flagellotropic tailed bacteriophages |
title_sort | architecture and stabilisation of flagellotropic tailed bacteriophages |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7385642/ https://www.ncbi.nlm.nih.gov/pubmed/32719311 http://dx.doi.org/10.1038/s41467-020-17505-w |
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