An essential role for the baseplate protein Gp45 in phage adsorption to Staphylococcus aureus.
In: Scientific reports, Jg. 6 (2016-05-23), S. 26455
Online
academicJournal
Zugriff:
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.
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An essential role for the baseplate protein Gp45 in phage adsorption to Staphylococcus aureus.
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Autor/in / Beteiligte Person: | Li, X ; Koç, C ; Kühner, P ; Stierhof, YD ; Krismer, B ; Enright, MC ; Penadés, JR ; Wolz, C ; Stehle, T ; Cambillau, C ; Peschel, A ; Xia, G |
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Zeitschrift: | Scientific reports, Jg. 6 (2016-05-23), S. 26455 |
Veröffentlichung: | London : Nature Publishing Group, copyright 2011-, 2016 |
Medientyp: | academicJournal |
ISSN: | 2045-2322 (electronic) |
DOI: | 10.1038/srep26455 |
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