Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

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Record number 359227
Title Intermolecular forces and enthalpies in the adhesion of Streptococcus mutans and antigen I/II deficient mutant to laminin films
Author(s) Busscher, H.J.; Belt-Gritter, B. van de; Dijkstra, R.J.B.; Norde, W.; Mei, H.C. van der
Source Journal of Bacteriology 189 (2007)8. - ISSN 0021-9193 - p. 2988 - 2995.
DOI https://doi.org/10.1128/JB.01731-06
Department(s) Physical Chemistry and Colloid Science
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2007
Keyword(s) major surface protein - oral bacterial pairs - antibody interaction - isogenic mutants - concanavalin-a - serotype-c - microscopy - binding - aggregation - intermedius
Abstract The antigen I/II family of surface proteins is expressed by most oral streptococci, including Streptococcus mutans, and mediates specific adhesion to, among other things, salivary films and extracellular matrix proteins. In this study we showed that antigen I/II-deficient S. mutans isogenic mutant IB03987 was nearly unable to adhere to laminin films under flow conditions due to a lack of specific interactions (0.8 x 106 and 1.1 x 106 cells cm¿2 at pH 5.8 and 6.8, respectively) compared with parent strain LT11 (21.8 x 106 and 26.1 x 106 cells cm¿2). The adhesion of both the parent and mutant strains was slightly greater at pH 6.8 than at pH 5.8. In addition, atomic force microscopy (AFM) experiments demonstrated that the parent strain experienced less repulsion when it approached a laminin film than the mutant experienced. Upon retraction, combined specific and nonspecific adhesion forces were stronger for the parent strain (up to ¿5.0 and ¿4.9 nN at pH 5.8 and 6.8, respectively) than for the mutant (up to ¿1.5 and ¿2.1 nN), which was able to interact only through nonspecific interactions. Enthalpy was released upon adsorption of laminin to the surface of the parent strain but not upon adsorption of laminin to the surface of IB03987. A comparison of the adhesion forces in AFM with the adhesion forces reported for specific ligand-receptor complexes resulted in the conclusion that the number of antigen I/II binding sites for laminin on S. mutans LT11 is on the order of 6 x 104 sites per organism and that the sites are probably arranged along exterior surface structures, as visualized here by immunoelectron microscopy.
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