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Deciphering the role of monosaccharides during phage infection of Staphylococcus aureus
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International audience. As phages are extensively investigated as novel therapy tools but also as transfer agents for antibiotic resistance genes, thorough understanding of phage-host interactions becomes crucial. Prerequisite for phage infection is its adhesion to the host surface. Here, we used atomic force microscopy-based single-particle force spectroscopy with phage-decorated tips to decipher the adhesion of phage 187 on living Staphylococcus aureus cells. We found that addition of free N-acetyl-D-glucosamine was able to decrease phage adhesion, suggesting that this monosaccharide plays major role in phage 187 infection of S. aureus. Moreover, phage 187 adhesion on monosaccharide-coated model surfaces combined with plaque forming unit counts suggested that a direct link can be established between the propensity to bind to a saccharide and the capability of the latter to inhibit phage infection. On a nanoscale level, single-particle force spectroscopy was successfully used to identify a major receptor required for phage 187 infection of S. aureus but also evidenced that this receptor was responsible for phage adhesion on host-cells. Our work demonstrates that single-particle force spectroscopy is a powerful platform to screen and predict the molecular target of phages on their host surfaces.
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