Identification of dual receptor binding protein systems in Lactococcal 936 group phages

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dc.contributor.author Hayes, Stephen
dc.contributor.author Duhoo, Yoan
dc.contributor.author Neve, Horst
dc.contributor.author Murphy, James
dc.contributor.author Noben, Jean-Paul
dc.contributor.author Franz, Charles M. A. P.
dc.contributor.author Cambillau, Christian
dc.contributor.author Mahony, Jennifer
dc.contributor.author Nauta, Arjen
dc.contributor.author van Sinderen, Douwe
dc.date.accessioned 2019-06-26T16:19:51Z
dc.date.available 2019-06-26T16:19:51Z
dc.date.issued 2018
dc.identifier.citation Hayes, S., Duhoo, Y., Neve, H., Murphy, J., Noben, J.P., Franz, C., Cambillau, C., Mahony, J., Nauta, A. and van Sinderen, D., 2018. Identification of Dual Receptor Binding Protein Systems in Lactococcal 936 Group Phages. Viruses, 10(12): 668 (17pp) DOI: 10.3390/v10120668 en
dc.identifier.volume 10 en
dc.identifier.issued 12 en
dc.identifier.startpage 1 en
dc.identifier.endpage 17 en
dc.identifier.issn 1999-4915
dc.identifier.uri http://hdl.handle.net/10468/8106
dc.identifier.doi 10.3390/v10120668 en
dc.description.abstract Siphoviridae of the lactococcal 936 group are the most commonly encountered bacteriophages in the dairy processing environment. The 936 group phages possess a discrete baseplate at the tip of their tail—a complex harbouring the Receptor Binding Protein (RBP) which is responsible for host recognition and attachment. The baseplate-encoding region is highly conserved amongst 936 phages, with 112 of 115 publicly available phages exhibiting complete synteny. Here, we detail the three exceptions (Phi4.2, Phi4R15L, and Phi4R16L), which differ from this genomic architecture in possessing an apparent second RBP-encoding gene upstream of the “classical” rbp gene. The newly identified RBP possesses an elongated neck region relative to currently defined 936 phage RBPs and is genetically distinct from defined 936 group RBPs. Through detailed characterisation of the representative phage Phi4.2 using a wide range of complementary techniques, we demonstrated that the above-mentioned three phages possess a complex and atypical baseplate structure. Furthermore, the presence of both RBPs in the tail tip of the mature virion was confirmed, while the anticipated host-binding capabilities of both proteins were also verified. en
dc.description.sponsorship Irish Research Council (IRC Industry Partnership studentship); Hercules Stichting (R-3986) en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher MDPI en
dc.relation.uri https://www.mdpi.com/1999-4915/10/12/668
dc.rights © 2018 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 en
dc.rights.uri https://creativecommons.org/licenses/by/4.0/ en
dc.subject Virus en
dc.subject Lactic acid bacteria en
dc.subject Structure en
dc.subject Host interactions en
dc.title Identification of dual receptor binding protein systems in Lactococcal 936 group phages en
dc.type Article (peer-reviewed) en
dc.internal.authorcontactother Douwe Van Sinderen, School of Microbiology, 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 Science Foundation Ireland en
dc.contributor.funder Irish Research Council en
dc.contributor.funder Hercules Foundation en
dc.description.status Peer reviewed en
dc.identifier.journaltitle Viruses en
dc.internal.IRISemailaddress d.vansinderen@ucc.ie en
dc.identifier.articleid 668 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


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© 2018 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 Except where otherwise noted, this item's license is described as © 2018 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
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