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Viruses 2018, 10(12), 668;

Identification of Dual Receptor Binding Protein Systems in Lactococcal 936 Group Phages

School of Microbiology & APC Microbiome Ireland, University College Cork, Western Road, Cork T12 YT20, Ireland
Architecture et Fonction des Macromolécules Biologiques, Centre National de la Recherche Scientifique (CNRS), Campus de Luminy, 13288 Marseille, France
Department of Microbiology and Biotechnology, Max Rubner-Institut, 24103 Kiel, Germany
Biomedical Research Institute, Hasselt University, 3500 Diepenbeek, Belgium
Architecture et Fonction des Macromolécules Biologiques, Aix-Marseille Université, Campus de Luminy, 13288 Marseille, France
FrieslandCampina, 3818 Amersfoort, The Netherlands
Author to whom correspondence should be addressed.
Received: 28 September 2018 / Revised: 21 November 2018 / Accepted: 22 November 2018 / Published: 27 November 2018
(This article belongs to the Special Issue Viruses of Microbes V: Biodiversity and Future Applications)
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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. View Full-Text
Keywords: virus; lactic acid bacteria; structure; host interactions virus; lactic acid bacteria; structure; host interactions

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Hayes, S.; Duhoo, Y.; Neve, H.; Murphy, J.; Noben, J.-P.; Franz, C.M.A.P.; Cambillau, C.; Mahony, J.; Nauta, A.; Van Sinderen, D. Identification of Dual Receptor Binding Protein Systems in Lactococcal 936 Group Phages. Viruses 2018, 10, 668.

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