Nature Biotechnology
17, 42 - 47 (1999)
doi:10.1038/5213
A synthetic peptide adhesion epitope as a novel antimicrobial agentCharles G. Kelly1, 2, Justine S. Younson1, 2, Ban Y. Hikmat1, 2, Stephen M. Todryk1, Michael Czisch4, Parvez I. Haris5, Ian R. Flindall2, Craig Newby3, Anthony I. Mallet3, Julian K-C. Ma1, 2
& Thomas Lehner11
Department of Immunology, St. John's Institute of Dermatology,
United Medical and Dental Schools of Guy's and St. Thomas' Hospitals,
London SE1 9RT, UK. 2
Department of Oral Medicine and Pathology, St. John's
Institute of Dermatology, United Medical and Dental Schools of Guy's and St.
Thomas' Hospitals, London SE1 9RT, UK.
3
St. John's Institute of Dermatology, United Medical
and Dental Schools of Guy's and St. Thomas' Hospitals, London
SE1 9RT, UK. 4
Bijvoet Center for Biomolecular Research, Utrecht University,
The Netherlands. 5
Department of Biological Sciences, De Montfort University,
Leicester, UK.
Correspondence should be addressed to Charles G. Kelly (c.kelly@umds.ac.uk).bacterial adhesinantimicrobial peptideadhesion epitopesurface plasmon resonance
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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