Ubiquitous carbohydrate binding modules decorate 936 lactococcal siphophage virions

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dc.contributor.author Hayes, Stephen
dc.contributor.author Mahony, Jennifer
dc.contributor.author Vincentelli, Renaud
dc.contributor.author Ramond, Laurie
dc.contributor.author Nauta, Arjen
dc.contributor.author van Sinderen, Douwe
dc.contributor.author Cambillau, Christian
dc.date.accessioned 2019-10-23T04:34:10Z
dc.date.available 2019-10-23T04:34:10Z
dc.date.issued 2019-07-09
dc.identifier.citation Hayes, S., Mahony, J., Vincentelli, R., Ramond, L., Nauta, A., van Sinderen, D. and Cambillau, C. (2019) 'Ubiquitous Carbohydrate Binding Modules Decorate 936 Lactococcal Siphophage Virions', Viruses, 11(7), 631. (19pp.) DOI: 10.3390/v11070631 en
dc.identifier.volume 11 en
dc.identifier.issued 7 en
dc.identifier.startpage 1 en
dc.identifier.endpage 19 en
dc.identifier.uri http://hdl.handle.net/10468/8829
dc.identifier.doi 10.3390/v11070631 en
dc.description.abstract With the availability of an increasing number of 3D structures of bacteriophage components, combined with powerful in silico predictive tools, it has become possible to decipher the structural assembly and functionality of phage adhesion devices. In the current study, we examined 113 members of the 936 group of lactococcal siphophages, and identified a number of Carbohydrate Binding Modules (CBMs) in the neck passage structure and major tail protein, on top of evolved Dit proteins, as recently reported by us. The binding ability of such CBM-containing proteins was assessed through the construction of green fluorescent protein fusion proteins and subsequent binding assays. Two CBMs, one from the phage tail and another from the neck, demonstrated definite binding to their phage-specific host. Bioinformatic analysis of the structural proteins of 936 phages reveals that they incorporate binding modules which exhibit structural homology to those found in other lactococcal phage groups and beyond, indicating that phages utilize common structural “bricks” to enhance host binding capabilities. The omnipresence of CBMs in Siphophages supports their beneficial role in the infection process, as they can be combined in various ways to form appendages with different shapes and functionalities, ensuring their success in host detection in their respective ecological niches. en
dc.description.sponsorship French Infrastructure for Integrated Structural Biology (FRISBI ANR-10-INSB-05-01) en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher MDPI AG en
dc.relation.uri https://www.mdpi.com/1999-4915/11/7/631/htm
dc.rights © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). en
dc.rights.uri http://creativecommons.org/licenses/by/4.0/ en
dc.subject Bacteriophage en
dc.subject Lactococcus lactis en
dc.subject Receptor-binding protein en
dc.subject Carbohydrate binding module en
dc.subject Phage-host interactions en
dc.title Ubiquitous carbohydrate binding modules decorate 936 lactococcal siphophage virions en
dc.type Article (peer-reviewed) en
dc.internal.authorcontactother Douwe van Sinderen, School of Microbiology and APC Microbiome Ireland, University College Cork, Cork, Ireland. +353-21-490-3000 Email:d.vansinderen@ucc.ie en
dc.internal.availability Full text available en
dc.description.version Published Version en
dc.contributor.funder Irish Research Council en
dc.contributor.funder Science Foundation Ireland en
dc.contributor.funder French Infrastructure for Integrated Structural Biology en
dc.description.status Peer reviewed en
dc.identifier.journaltitle Viruses en
dc.internal.IRISemailaddress d.vansinderen@ucc.ie en
dc.identifier.articleid 631 en
dc.relation.project info:eu-repo/grantAgreement/SFI/SFI Starting Investigator Research Grant (SIRG)/15/SIRG/3430/IE/Phage-host interactome of the dairy bacterium Streptococcus thermophilus (PHIST)/ en
dc.relation.project info:eu-repo/grantAgreement/SFI/SFI Investigator Programme/13/IA/1953/IE/Functional analysis of the host adsorption and DNA injection processes of a lactococcal bacteriophage/ en
dc.identifier.eissn 1999-4915


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© 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). Except where otherwise noted, this item's license is described as © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
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