A structural discovery journey of streptococcal phages adhesion devices by AlphaFold2

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Date
2022-08-19
Authors
Goulet, Adeline
Joos, Raphaela
Lavelle, Katherine
van Sinderen, Douwe
Mahony, Jennifer
Cambillau, Christian
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Frontiers Media S.A.
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Abstract
Successful 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.
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Keywords
Bacteriophage , Streptococcus , AlphaFold2 , Phage-host interactions , Carbohydrate-binding module , Receptor-binding protein
Citation
Goulet, 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.2022.960325