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Viruses. 2019 Jul 9;11(7). pii: E631. doi: 10.3390/v11070631.

Ubiquitous Carbohydrate Binding Modules Decorate 936 Lactococcal Siphophage Virions.

Author information

1
School of Microbiology, University College Cork, T12 YT20 Cork, Ireland.
2
Architecture et Fonction des Macromolécules Biologiques, Aix-Marseille Université, Campus de Luminy, 12388 Marseille, France.
3
Architecture et Fonction des Macromolécules Biologiques, Centre National de la Recherche Scientifique (CNRS), Campus de Luminy, 13288 Marseille, France.
4
FrieslandCampina, 3800 Amersfoort, The Netherlands.
5
School of Microbiology, University College Cork, T12 YT20 Cork, Ireland. d.vansinderen@ucc.ie.
6
APC Microbiome Ireland, University College Cork, T12 YT20 Cork, Ireland. d.vansinderen@ucc.ie.
7
School of Microbiology, University College Cork, T12 YT20 Cork, Ireland. ccambillau@gmail.com.
8
Architecture et Fonction des Macromolécules Biologiques, Aix-Marseille Université, Campus de Luminy, 12388 Marseille, France. ccambillau@gmail.com.
9
Architecture et Fonction des Macromolécules Biologiques, Centre National de la Recherche Scientifique (CNRS), Campus de Luminy, 13288 Marseille, France. ccambillau@gmail.com.

Abstract

With the availability of an increasing number of 3D structures of bacteriophage components, combined with powerful in silico predictive tools, it has become possible to decipher the structural assembly and functionality of phage adhesion devices. In the current study, we examined 113 members of the 936 group of lactococcal siphophages, and identified a number of Carbohydrate Binding Modules (CBMs) in the neck passage structure and major tail protein, on top of evolved Dit proteins, as recently reported by us. The binding ability of such CBM-containing proteins was assessed through the construction of green fluorescent protein fusion proteins and subsequent binding assays. Two CBMs, one from the phage tail and another from the neck, demonstrated definite binding to their phage-specific host. Bioinformatic analysis of the structural proteins of 936 phages reveals that they incorporate binding modules which exhibit structural homology to those found in other lactococcal phage groups and beyond, indicating that phages utilize common structural "bricks" to enhance host binding capabilities. The omnipresence of CBMs in Siphophages supports their beneficial role in the infection process, as they can be combined in various ways to form appendages with different shapes and functionalities, ensuring their success in host detection in their respective ecological niches.

KEYWORDS:

Lactococcus lactis; bacteriophage; carbohydrate binding module; phage–host interactions; receptor-binding protein

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