Molecular force probe measurement of antigen I/II–matrix protein interactions

Authors

  • Martine Soell,

    1. Department of Periodontology, Dental Faculty Strasbourg, Hautepierre Hospitals, Strasbourg, University, Strasbourg
    2. INSERM U 977, Strasbourg, France
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    • Authors who contributed equally to the work presented in this article.

  • Joseph Hemmerlé,

    1. INSERM U 977, Strasbourg, France
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    • Authors who contributed equally to the work presented in this article.

  • Matthias Hannig,

    1. Clinic of Operative Dentistry, Periodontology and Preventive Dentistry, Saarland University Hospitals, Homburg/Saar, Germany
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  • Youssef Haïkel,

    1. INSERM U 977, Strasbourg, France
    2. Department of Restorative Dentistry and Endodontology, Dental Faculty Strasbourg, Strasbourg University, Strasbourg, France
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  • Hidehiko Sano,

    1. Department of Restorative Dentistry, Division of Oral Health Science, Graduate School of Dental Medicine, Hokkaido University, Sapporo, Japan
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  • Denis Selimovic

    1. INSERM U 977, Strasbourg, France
    2. Department of Oral Medicine and Surgery, Dental Faculty Strasbourg, Strasbourg University, Strasbourg, France
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Denis Selimovic, Department of Oral Medicine and Surgery, Dental Faculty Strasbourg, Strasbourg University, INSERM U 977, 11 Rue Humann, 67085 Strasbourg, France
Telefax: +33–3–68853223
E-mail: denis.selimovic@t-online.de

Abstract

Soell M, Hemmerlé J, Hannig M, Haïkel Y, Sano H, Selimovic D. Molecular force probe measurement of antigen I/II–matrix protein interactions. Eur J Oral Sci 2010; 118: 590–595. © 2010 Eur J Oral Sci

Viridans streptococci possess a family of immunologically and structurally related cell-surface proteins, termed antigen I/II, which may function as adhesins and enable oral streptococci to adhere to saliva-coated surfaces and matrix proteins. Here we used atomic force microscopy in the molecular force mode to measure the specific interaction forces between antigen I/II and two matrix proteins, collagen and fibronectin. These matrix proteins provide important binding sites for adherence of oral streptococcal in dentinal caries and endocarditis, respectively. Antigen I/II-coated cantilever tips were brought into contact with collagen- or fibronectin-coated silica coverslips. For the protein I/II–fibronectin interaction experiments, the mean strength of the last ruptures was 216 pN, with most of the detachments located around 125 pN. In antigen I/II–collagen interaction experiments, the mean strength of the last rupture forces corresponded to 136 pN, with the most frequent unbinding force around 75 pN. Thus, our findings definitely suggest that, under the present experimental conditions, antigen I/II binds more strongly to fibronectin than to type I collagen. This might be of relevance for the attachment of viridians streptococci to surfaces exposed to strong hydrodynamic shearing forces under in vivo conditions.

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