An essential role for the baseplate protein Gp45 in phage adsorption to Staphylococcus aureus

Xuehua Li, Cengiz Koç, Petra Kühner, York-Dieter Stierhof, Bernhard Krismer, Mark C. Enright, José R. Penadés, Christiane Wolz, Thilo Stehle, Christian Cambillau, Andreas Peschel, Guoqing Xia

Research output: Contribution to journalArticlepeer-review


Despite the importance of phages in driving horizontal gene transfer (HGT) among pathogenic bacteria, the underlying molecular mechanisms mediating phage adsorption to S. aureus are still unclear. Phage ϕ11 is a siphovirus with a high transducing efficiency. Here, we show that the tail protein Gp45 localized within the ϕ11 baseplate. Phage ϕ11 was efficiently neutralized by anti-Gp45 serum, and its adsorption to host cells was inhibited by recombinant Gp45 in a dose-dependent manner. Flow cytometry analysis demonstrated that biotin-labelled Gp45 efficiently stained the wild-type S. aureus cell but not the double knockout mutant ΔtarM/S, which lacks both α- and β-O-GlcNAc residues on its wall teichoic acids (WTAs). Additionally, adsorption assays indicate that GlcNAc residues on WTAs and O-acetyl groups at the 6-position of muramic acid residues in peptidoglycan are essential components of the ϕ11 receptor. The elucidation of Gp45-involved molecular interactions not only broadens our understanding of siphovirus-mediated HGT, but also lays the groundwork for the development of sensitive affinity-based diagnostics and therapeutics for S. aureus infection.
Original languageEnglish
Article number26455
JournalScientific Reports
Early online date23 May 2016
Publication statusPublished - 23 May 2016


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