Adsorption of Staphylococcus viruses S13' and S24-1 on staphylococcus aureus strains with different glycosidic linkage patterns of wall teichoic acids

Jumpei Uchiyama, Maya Taniguchi, Kenji Kurokawa, Iyo Takemura-Uchiyama, Takako Ujihara, Hidekatsu Shimakura, Yoshihiko Sakaguchi, Hironobu Murakami, Masahiro Sakaguchi, Shigenobu Matsuzaki

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)

Abstract

The group of phages belonging to the family Podoviridae, genus P68virus, including Staphylococcus viruses S13' and S24-1, are important because of their benefits in phage therapy against Staphylococcus aureus infections. The O-glycosidic linkage patterns of wall teichoic acids (WTAs) in S. aureus cell walls seem to be important for adsorption of this phage group. In this study, the adsorption of Staphylococcus viruses S13' and S24-1 to S. aureus was examined using strains with modified WTA glycosidic linkage patterns. We found that the β-O-N-acetylglucosamine of WTAs was essential for S13' adsorption, while Nacetylglucosamine, regardless of the α- and β-O-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-O-N-acetylglucosamine of the WTAs was essential for S13' RBP binding, while N-acetylglucosamine, regardless of the a- and β-O-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 Staphylococcus viruses S13' and S24-1 were structurally similar to the RBPs of phage phi11 of thefamily Siphoviridae. Phylogenetic analysis of the RBPs indicated that two phylogenetic subclusters in the family Podoviridae 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.

Original languageEnglish
Article number000865
Pages (from-to)2171-2180
Number of pages10
JournalJournal of General Virology
Volume98
Issue number8
DOIs
Publication statusPublished - Aug 2017
Externally publishedYes

Keywords

  • Adsorption
  • N-acetylglucosamine
  • Podophage
  • Receptor-binding protein
  • Wall teichoic acids

ASJC Scopus subject areas

  • Virology

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