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

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 attachme...

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Bibliographic Details
Published in:Viruses 2018-11, Vol.10 (12), p.668
Main Authors: Hayes, Stephen, Duhoo, Yoan, Neve, Horst, Murphy, James, Noben, Jean-Paul, Franz, Charles M A P, Cambillau, Christian, Mahony, Jennifer, Nauta, Arjen, van Sinderen, Douwe
Format: Article
Language:English
Subjects:
Adsorption
Amino Acid Sequence
Bacteriophages - physiology
Bacteriophages - ultrastructure
Biochemistry
Biochemistry, Molecular Biology
Biological Products
Cloning
Gene expression
Genome, Viral
Genomes
Gram-positive bacteria
host interactions
Host Microbial Interactions
lactic acid bacteria
Lactococcus lactis - virology
Life Sciences
Mass spectrometry
Microscopy
Models, Molecular
Open Reading Frames
Phages
Protein Conformation
Proteins
Scientific imaging
structure
Synteny
Viral Proteins - chemistry
Viral Proteins - genetics
Viral Proteins - metabolism
Virions
virus
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Summary: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" 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.
ISSN:1999-4915
1999-4915
DOI:10.3390/v10120668