dc.contributor.author	Lavelle, Katherine
dc.contributor.author	Goulet, Adeline
dc.contributor.author	McDonnell, Brian
dc.contributor.author	Spinelli, Silvia
dc.contributor.author	van Sinderen, Douwe
dc.contributor.author	Mahony, Jennifer
dc.contributor.author	Cambillau, Christian
dc.contributor.funder	Science Foundation Ireland	en
dc.contributor.funder	French Infrastructure for Integrated Structural Biology	en
dc.date.accessioned	2022-04-08T13:59:38Z
dc.date.available	2022-04-08T13:59:38Z
dc.date.issued	2020-01
dc.date.updated	2022-04-08T13:24:36Z
dc.description.abstract	Available 3D structures of bacteriophage modules combined with predictive bioinformatic algorithms enabled the identification of adhesion modules in 57 siphophages infecting Streptococcus thermophilus (St). We identified several carbohydrate-binding modules (CBMs) in so-called evolved distal tail (Dit) and tail-associated lysozyme (Tal) proteins of St phage baseplates. We examined the open reading frame (ORF) downstream of the Tal-encoding ORF and uncovered the presence of a putative p2-like receptor-binding protein (RBP). A 21 Å resolution electron microscopy structure of the baseplate of cos-phage STP1 revealed the presence of six elongated electron densities, surrounding the core of the baseplate, that harbour the p2-like RBPs at their tip. To verify the functionality of these modules, we expressed GFP- or mCherry-coupled Tal and putative RBP CBMs and observed by fluorescence microscopy that both modules bind to their corresponding St host, the putative RBP CBM with higher affinity than the Tal-associated one. The large number of CBM functional domains in St phages suggests that they play a contributory role in the infection process, a feature that we previously described in lactococcal phages and beyond, possibly representing a universal feature of the siphophage host-recognition apparatus.	en
dc.description.sponsorship	French Infrastructure for Integrated Structural Biology (Grant number ANR-10-INSB-05-01)	en
dc.description.status	Peer reviewed	en
dc.description.version	Published Version	en
dc.format.mimetype	application/pdf	en
dc.identifier.citation	Lavelle, K., Goulet, A., McDonnell, B., Spinelli, S., van Sinderen, D., Mahony, J. and Cambillau, C. (2020) 'Revisiting the host adhesion determinants of Streptococcus thermophilus siphophages', Microbial Biotechnology, 13(6), pp.1765-1779. doi: 10.1111/1751-7915.13593	en
dc.identifier.doi	10.1111/1751-7915.13593	en
dc.identifier.endpage	1779	en
dc.identifier.issn	1751-7907
dc.identifier.issued	6	en
dc.identifier.journaltitle	Microbial Biotechnology	en
dc.identifier.startpage	1765	en
dc.identifier.uri	https://hdl.handle.net/10468/13050
dc.identifier.volume	13	en
dc.language.iso	en	en
dc.publisher	John Wiley & Sons, Inc.	en
dc.relation.project	info:eu-repo/grantAgreement/SFI/SFI Starting Investigator Research Grant (SIRG)/15/SIRG/3430/IE/Phage-host interactome of the dairy bacterium Streptococcus thermophilus (PHIST)/	en
dc.relation.project	info:eu-repo/grantAgreement/SFI/SFI Investigator Programme/13/IA/1953/IE/Functional analysis of the host adsorption and DNA injection processes of a lactococcal bacteriophage/	en
dc.rights	© 2020 The Authors. Microbial Biotechnologypublished by John Wiley & Sons Ltd and Society for Applied Microbiology.This is an open access article under the terms of the Creative Commons Attribution-NonCommercial License, which permits use,distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.	en
dc.rights.uri	https://creativecommons.org/licenses/by/4.0/	en
dc.subject	Streptococcus thermophilus siphophages	en
dc.subject	3D structures	en
dc.subject	Bacteriophage modules	en
dc.subject	Carbohydrate-binding modules	en
dc.subject	CBMs	en
dc.title	Revisiting the host adhesion determinants of Streptococcus thermophilus siphophages	en
dc.type	Article (peer-reviewed)	en

Revisiting the host adhesion determinants of Streptococcus thermophilus siphophages

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