1887

Abstract

The group of phages belonging to the family genus , including viruses S13′ and S24-1, are important because of their benefits in phage therapy against infections. The -glycosidic linkage patterns of wall teichoic acids (WTAs) in cell walls seem to be important for adsorption of this phage group. In this study, the adsorption of viruses S13′ and S24-1 to was examined using strains with modified WTA glycosidic linkage patterns. We found that the β--N-acetylglucosamine of WTAs was essential for S13 adsorption, while N-acetylglucosamine, regardless of the α- and β--glycosidic linkages of the WTAs, was essential for S24-1 adsorption. Next, examining the binding activities of their receptor-binding proteins (RBPs) to cell walls with different WTA glycosidic patterns, the β--N-acetylglucosamine of the WTAs was essential for S13 RBP binding, while N-acetylglucosamine, regardless of the α- and β--glycosidic linkages of the WTAs, was essential for S24-1 RBP binding. Therefore, the results of the RBP binding assays were consistent with those of the phage adsorption assays. Bioinformatic analysis suggested that the RBPs of viruses S13′ and S24-1 were structurally similar to the RBPs of phage phi11 of thefamily . Phylogenetic analysis of the RBPs indicated that two phylogenetic subclusters in the family were related to the glycosidic linkage patterns required for phage adsorption, possibly mediated by RBPs. We hope that this study will encourage the future development of therapeutic phages.

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2017-08-01
2024-04-18
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