A structural discovery journey of streptococcal phages adhesion devices by AlphaFold2

By A. Goulet, R. Joos, K. Lavelle, D. van Sinderen, J. Mahony, Christian Cambillau. 2022

17 citations recorded by the source corpus.

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.

Subfields: Ecology, Molecular Biology, Radiology, Nuclear Medicine and Imaging

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In Molecular Biology

1. D. van Sinderen
2. J. Mahony
3. A. Goulet
4. Christian Cambillau

Citations in the corpus

• Exploring Structural Diversity among Adhesion Devices Encoded by Lactococcal P335 Phages with AlphaFold2 (2022, background): “It is followed by a short trimeric collagen-like linker and a so-called 3β domain previously observed in streptococcal phages [20].”