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Title: | Identification of Dual Receptor Binding ProteinSystems in Lactococcal 936 Group Phages. | Authors: | Hayes, S. Duhoo, Y. Neve, H. Murphy, J. NOBEN, Jean-Paul Franz, C.M.A.P. Cambillau, C. Mahony, J. Nauta, A. van Sinderen, D. |
Issue Date: | 2018 | Source: | Viruses-Basel, 10(12) (Art N° 668) | 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. | Notes: | van Sinderen, D (reprint author), Univ Coll Cork, Sch Microbiol, Western Rd, Cork T12 YT20, Ireland. Univ Coll Cork, APC Microbiome Ireland, Western Rd, Cork T12 YT20, Ireland. stephen.hayes@umail.ucc.ie; Yoan.Duhoo@afmb.univ-mrs.fr; horst.neve@mri.bund.de; james.murphy@umail.ucc.ie; jeanpaul.noben@uhasselt.be; charles.franz@mri.bund.de; cambillau@afmb.univ-mrs.fr; j.mahony@ucc.ie; arjen.nauta@frieslandcampina.com; d.vansinderen@ucc.ie | Keywords: | virus; lactic acid bacteria; structure; host interactions | Document URI: | http://hdl.handle.net/1942/27783 | e-ISSN: | 1999-4915 | DOI: | 10.3390/v10120668 | ISI #: | 000455313100007 | Rights: | Copyright 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 (http://creativecommons.org/licenses/by/4.0/). | Category: | A1 | Type: | Journal Contribution | Validations: | ecoom 2020 |
Appears in Collections: | Research publications |
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viruses-10-00668.pdf | Published version | 6.93 MB | Adobe PDF | View/Open |
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