Ministry of Agriculture, Forestry and Fisheries (MAFF)
GD0696J004
Japan
Japan Society for the Promotion of Science (JSPS)
21K20645
Japan
Citation
Journal: Sci Adv / Year: 2025 Title: Cryo-EM structure of bacteriophage Bas63 reveals structural conservation and diversity in the genus. Authors: James Hodgkinson-Bean / Rafael Ayala / Klemens McJarrow-Keller / Léna Cassin / Georgia L Rutter / Alexander J M Crowe / Matthias Wolf / Mihnea Bostina / Abstract: The BASEL phage collection was developed to provide access to diverse bacteriophages, distinct from model phages. phage JohannRWettstein (Bas63), a myophage in the collection, is a member of the ...The BASEL phage collection was developed to provide access to diverse bacteriophages, distinct from model phages. phage JohannRWettstein (Bas63), a myophage in the collection, is a member of the subfamily Ounavirinae and the genus. Using cryo-electron microscopy, we investigated Bas63's structure to explore its evolutionary relationships and functional adaptations. Our structures reveal a series of gene products: (i) a capsid decorated with β-tulip proteins at three-fold symmetry axes and a Hoc-like protein at hexamer centers, (ii) a conserved connector with an additional 12-fold ring of collar proteins that extend unique whisker proteins that are structurally related to podophage GP4 tail fibers, and (iii) a baseplate with long tail fibers resembling a contracted form of T4's long tail fibers. Sequence conservation analysis of Bas63 structural proteins across ICTV-recognized supports its role as a structural model for evolution. This study advances the mechanistic understanding of phage architecture and reinforces the structural mosaicism of bacteriophages.
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