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

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dc.contributor.authorHayes, Stephen
dc.contributor.authorDuhoo, Yoan
dc.contributor.authorNeve, Horst
dc.contributor.authorMurphy, James
dc.contributor.authorNoben, Jean-Paul
dc.contributor.authorFranz, Charles M. A. P.
dc.contributor.authorCambillau, Christian
dc.contributor.authorMahony, Jennifer
dc.contributor.authorNauta, Arjen
dc.contributor.authorvan Sinderen, Douwe
dc.contributor.funderScience Foundation Irelanden
dc.contributor.funderIrish Research Councilen
dc.contributor.funderHercules Foundationen
dc.date.accessioned2019-06-26T16:19:51Z
dc.date.available2019-06-26T16:19:51Z
dc.date.issued2018
dc.description.abstractSiphoviridae 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.sponsorshipIrish Research Council (IRC Industry Partnership studentship); Hercules Stichting (R-3986)en
dc.description.statusPeer revieweden
dc.description.versionPublished Versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.articleid668en
dc.identifier.citationHayes, 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/v10120668en
dc.identifier.doi10.3390/v10120668en
dc.identifier.endpage17en
dc.identifier.issn1999-4915
dc.identifier.issued12en
dc.identifier.journaltitleVirusesen
dc.identifier.startpage1en
dc.identifier.urihttps://hdl.handle.net/10468/8106
dc.identifier.volume10en
dc.language.isoenen
dc.publisherMDPIen
dc.relation.projectinfo: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.projectinfo: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.relation.urihttps://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) licenseen
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en
dc.subjectVirusen
dc.subjectLactic acid bacteriaen
dc.subjectStructureen
dc.subjectHost interactionsen
dc.titleIdentification of dual receptor binding protein systems in Lactococcal 936 group phagesen
dc.typeArticle (peer-reviewed)en
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