Department of Microbiology, Moyne Institute of Preventive Medicine, School of Genetics and Microbiology, Trinity College Dublin, Dublin 2, Ireland.
Louvain Institute of Biomolecular Science and Technology, UC Louvain, Croix du Sud, 4-5, bte L7.07.07, B-1348, Louvain-la-Neuve, Belgium.
Nat Commun. 2022 May 6;13(1):2517. doi: 10.1038/s41467-022-30271-1.
Colonisation of humans by Staphylococcus aureus is a major risk factor for infection, yet the bacterial and host factors involved are not fully understood. The first step during skin colonisation is adhesion of the bacteria to corneocytes in the stratum corneum where the cornified envelope protein loricrin is the main ligand for S. aureus. Here we report a novel loricrin-binding protein of S. aureus, the cell wall-anchored fibronectin binding protein B (FnBPB). Single-molecule force spectroscopy revealed both weak and ultra-strong (2 nN) binding of FnBPB to loricrin and that mechanical stress enhanced the strength of these bonds. Treatment with a peptide derived from fibrinogen decreased the frequency of strong interactions, suggesting that both ligands bind to overlapping sites within FnBPB. Finally, we show that FnBPB promotes adhesion to human corneocytes by binding strongly to loricrin, highlighting the relevance of this interaction to skin colonisation.
金黄色葡萄球菌对人类的定植是感染的一个主要危险因素,但涉及的细菌和宿主因素尚未完全了解。细菌在皮肤定植的第一步是与角质层中的角蛋白细胞黏附,其中角蛋白丝聚合蛋白是金黄色葡萄球菌的主要配体。在这里,我们报告了金黄色葡萄球菌的一种新型角蛋白丝聚合蛋白结合蛋白 B(FnBPB)。单分子力谱技术显示,FnBPB 与角蛋白丝聚合蛋白的结合具有弱结合和超强结合(2 nN)的特点,机械应力增强了这些结合的强度。用源自纤维蛋白原的肽处理降低了强相互作用的频率,这表明两种配体结合到 FnBPB 的重叠位点。最后,我们表明 FnBPB 通过与角蛋白丝聚合蛋白强烈结合促进对人角蛋白细胞的黏附,这突出了这种相互作用与皮肤定植的相关性。