Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Detection and Kinetics of Mucosal Pathogenic Bacteria Binding with Polysaccharides

  • Chung, Kyong-Hwan (Center for Functional Nano Fine Chemicals (Post BK21 Program), Chonnam National University) ;
  • Park, Jung-Soon (Department of Material and Biochemical Engineering, Chonnam National University) ;
  • Hwang, Hyun-Soo (Department of Material and Biochemical Engineering, Chonnam National University) ;
  • Kim, Jin-Chul (School of Biotechnology & Bioengineering, Kangwon National University) ;
  • Lee, Ki-Young (Center for Functional Nano Fine Chemicals (Post BK21 Program), Chonnam National University)
  • Published : 2007.07.31
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Abstract

The detection and kinetics of mucosal pathogenic bacteria binding on polysaccharide ligands were studied using a surface plasmon resonance biosensor. The kinetic model applied curve-fitting to the experimental surface plasmon resonance sensorgrams to evaluate the binding interactions. The kinetic parameters for the mucosal pathogenic bacteria (Pseudomonas aeruginosa, Pseudomonas fluorescens, Serratia marcescens) with the alginate ligand were determined from a kinetic model. In addition, the binding interactions of the mucosal pathogenic bacteria with polysaccharide binding pairs (Pseudomonas aeruginosa/alginate, Streptococcus pneumoniae/pneumococcal polysaccharide, Staphylococcus aureus/pectin) were also compared with their kinetic parameters. The rate constants of association for Pseudomonas aeruginosa with the alginate ligand were higher than those for Pseudomonas fluorescens. Serratia marcescens had no detectable interaction with the alginate ligand. The adhesion affinity of Pseudomonas aeruginosa with alginate was higher than that for the other binding pairs. The binding affinities of the pathogenic bacteria with their own polysaccharide were higher than that of Staphylococcus aureus with pectin. Measuring the contact angle was found to be a feasible method for detecting binding interactions between analytes and ligands.

Keywords

References

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