Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Ubiquitous Carbohydrate Binding Modules Decorate 936 Lactococcal Siphophage Virions

Stephen Hayes
ORCID logo ,
Jennifer Mahony
,
Renaud Vincentelli
,
Laurie Ramond
,
Arjen Nauta
,
Douwe Sinderen
,
Christian CAMBILLAU
* ORCID logo
Version 1 : Received: 1 July 2019 / Approved: 2 July 2019 / Online: 2 July 2019 (11:45:19 CEST)

How to cite: Hayes, S.; Mahony, J.; Vincentelli, R.; Ramond, L.; Nauta, A.; Sinderen, D.; CAMBILLAU, C. Ubiquitous Carbohydrate Binding Modules Decorate 936 Lactococcal Siphophage Virions. Preprints 2019, 2019070044. https://doi.org/10.20944/preprints201907.0044.v1 Hayes, S.; Mahony, J.; Vincentelli, R.; Ramond, L.; Nauta, A.; Sinderen, D.; CAMBILLAU, C. Ubiquitous Carbohydrate Binding Modules Decorate 936 Lactococcal Siphophage Virions. Preprints 2019, 2019070044. https://doi.org/10.20944/preprints201907.0044.v1

Abstract

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

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

Subject

Biology and Life Sciences, Virology

Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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