Abstract
The earliest step in microbial infection is adherence by specific microbial adhesins to the mucosa of the oro-intestinal, nasorespiratory, or genitourinary tract. We inhibited binding of a cell surface adhesin of Streptococcus mutans to salivary receptors in vitro, as measured by surface plasmon resonance, using a synthetic peptide (p1025) corresponding to residues 1025–1044 of the adhesin. Two residues within p1025 that contribute to binding (Q1025, E1037) were identified by site-directed mutagenesis. In an in vivo human streptococcal adhesion model, direct application of p1025 to the teeth prevented recolonization of S. mutans but not Actinomyces , as compared with a control peptide or saline. This novel antimicrobial strategy, applying competitive peptide inhibitors of adhesion, may be used against other microorganisms in which adhesins mediate colonization of mucosal surfaces.
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Acknowledgements
This work was supported by the Wellcome Trust grant 040412 and the Special Funds of Guy's Hospital Dental School. NMR spectroscopic studies were supported by the TMR program "Access to Large-Scale Facilities" of the EC (ERBFMGECT950032). The BIAcore facility was established with funds from the Special Trustees of Guy's Hospital and the Special Trustees for St. Thomas' Hospital.
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Kelly, C., Younson, J., Hikmat, B. et al. A synthetic peptide adhesion epitope as a novel antimicrobial agent. Nat Biotechnol 17, 42–47 (1999). https://doi.org/10.1038/5213
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DOI: https://doi.org/10.1038/5213
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