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To develop a novel high-throughput tool for monitoring specific affinity of microbes with lectins, a kind of lectin microarray has been fabricated by immobilizing lectins on epoxide-derivatized glass slides and used to capture microbes. The capturing events are marked by attachment of lectin-conjugated gold nanoparticles followed by silver deposition to enhance the resonance light scattering (RLS) of the particles. The interactions of 16 lectins with four bacteria and one fungus were proffled by this approach. We demonstrated that the gold-nanoparticle-labeled array was suitable for identifying the binding affinity of lectin with bacterium, as well as determining the bacterium with high sensitivity. More importantly, we found that the growth of microbial strains in different culture media resulted in significant changes in their binding affinities with lectins, which might be important to the pathogenesis of the organisms. [ABSTRACT FROM AUTHOR]

In order to develop a novel high-throughput tool for monitoring carbohydrate-protein interactions, we prepared carbohydrate or glycoprotein microarrays by immobilizing amino modified carbohydrates on aldehyde- derivatized glass slides or glycoprotein on epoxide-derivatized glass slides and carried out lectin binding experiments by using these microarrays, respectively. The interaction events are marked by attachment of gold nanoparticles followed by silver deposition for signal enhancement. The attachment of the gold nanoparticles is achieved by standard avidin-biotin chemistry. The detection principle is resonance light scattering (RLS). The well-defined recognition systems, namely, three monosaccharides (Man-α, Glc-β and Gal-β) or three glycoproteins (Asf, RNase A and RNase B) with two lectins (ConA and RCA120), were chosen here to establish the RLS assay, respectively. Highly selective recognition of carbohydrate-protein down to 25.6 pg/mL for RCA120 in solution and 8 μM for Gal-β and 32 ng/mL for Asf on the microarray spots is demonstrated. [ABSTRACT FROM AUTHOR]