High-Affinity Interaction between the S-Layer Protein SbsC and the Secondary Cell Wall Polymer of<i>Geobacillus stearothermophilus</i>ATCC 12980 Determined by Surface Plasmon Resonance Technology

Abstract

Surface plasmon resonance studies using C-terminal truncation forms of the S-layer protein SbsC (recombinant SbsC consisting of amino acids 31 to 270 [rSbsC(31-270)] and rSbsC(31-443)) and the secondary cell wall polymer (SCWP) isolated from Geobacillus stearothermophilus ATCC 12980 confirmed the exclusive responsibility of the N-terminal region comprising amino acids 31 to 270 for SCWP binding. Quantitative analyses indicated binding behavior demonstrating low, medium, and high affinities.