期刊
ACS NANOSCIENCE AU
卷 3, 期 1, 页码 58-66出版社
AMER CHEMICAL SOC
DOI: 10.1021/acsnanoscienceau.2c00036
关键词
Staphylococcus aureus; FnBPB; corneodesmosin; extremely strong bonds; two-binding site mechanism
Attachment of Staphylococcus aureus to human skin corneocyte cells is mediated by bacterial cell-surface protein adhesins, including fibronectin-binding protein B (FnBPB). Using single-molecule experiments, it is demonstrated that FnBPB binds to corneodesmosin (CDSN) on atopic dermatitis patient corneocytes through a sophisticated two-site mechanism.
Attachment of Staphylococcus aureus to human skin corneocyte cells plays a critical role in exacerbating the severity of atopic dermatitis (AD). Pathogen-skin adhesion is mediated by bacterial cell-surface proteins called adhesins, including fibronectin-binding protein B (FnBPB). FnBPB binds to corneodesmosin (CDSN), a glycoprotein exposed on AD patient corneocytes. Using single-molecule experiments, we demonstrate that CDSN binding by FnBPB relies on a sophisticated two-site mechanism. Both sites form extremely strong bonds with binding forces of similar to 1 and similar to 2.5 nN albeit with faster dissociation rates than those reported for homologues of the adhesin. This previously unidentified two-binding site interaction in FnBPB illustrates its remarkable variety of adhesive functions and is of biological significance as the high strength and short bond lifetime will favor efficient skin colonization by the pathogen.
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