A structural discovery journey of streptococcal phages adhesion devices by AlphaFold2

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dc.contributor.authorGoulet, Adeline
dc.contributor.authorJoos, Raphaela
dc.contributor.authorLavelle, Katherine
dc.contributor.authorvan Sinderen, Douwe
dc.contributor.authorMahony, Jennifer
dc.contributor.authorCambillau, Christian
dc.contributor.funderScience Foundation Irelanden
dc.date.accessioned2022-09-30T10:32:04Z
dc.date.available2022-09-30T10:32:04Z
dc.date.issued2022-08-19
dc.date.updated2022-09-30T10:23:36Z
dc.description.abstractSuccessful bacteriophage infection starts with specific recognition and adhesion to the host cell surface. Adhesion devices of siphophages infecting Gram-positive bacteria are very diverse and remain, for the majority, poorly understood. These assemblies often comprise long, flexible, and multi-domain proteins, which limits their structural analyses by experimental approaches such as X-ray crystallography and electron microscopy. However, the protein structure prediction program AlphaFold2 is exquisitely adapted to unveil structural and functional details of such molecular machineries. Here, we present structure predictions of whole adhesion devices of five representative siphophages infecting Streptococcus thermophilus, one of the main lactic acid bacteria used in dairy fermentations. The predictions highlight the mosaic nature of these devices that share functional domains for which active sites and residues could be unambiguously identified. Such AlphaFold2 analyses of phage-encoded host adhesion devices should become a standard method to characterize phage-host interaction machineries and to reliably annotate phage genomes.en
dc.description.sponsorshipScience Foundation Ireland (Grant Numbers 20/FFP-P/8664; 12/RC/2273-P2)en
dc.description.statusPeer revieweden
dc.description.versionPublished Versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.articleid960325en
dc.identifier.citationGoulet, A., Joos, R., Lavelle, K., Van Sinderen, D., Mahony, J. and Cambillau, C. (2022) 'A structural discovery journey of streptococcal phages adhesion devices by AlphaFold2', Frontiers in Molecular Biosciences, 9, 960325 (9pp). doi: 10.3389/fmolb.2022.960325en
dc.identifier.doi10.3389/fmolb.2022.960325en
dc.identifier.eissn2296-889X
dc.identifier.endpage9en
dc.identifier.journaltitleFrontiers in Molecular Biosciencesen
dc.identifier.startpage1en
dc.identifier.urihttps://hdl.handle.net/10468/13712
dc.identifier.volume9en
dc.language.isoenen
dc.publisherFrontiers Media S.A.en
dc.relation.projectinfo: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.projectinfo: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© 2022, Goulet, Joos, Lavelle, Van Sinderen, Mahony and Cambillau. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.en
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en
dc.subjectBacteriophageen
dc.subjectStreptococcusen
dc.subjectAlphaFold2en
dc.subjectPhage-host interactionsen
dc.subjectCarbohydrate-binding moduleen
dc.subjectReceptor-binding proteinen
dc.titleA structural discovery journey of streptococcal phages adhesion devices by AlphaFold2en
dc.typeArticle (peer-reviewed)en
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