ZBiotech’s 100 Glycan Array (now CatchAll Glycan Array) helps scientists define the binding specificity of lectins.

In a groundbreaking exploration of the innate immune system of jawless vertebrates, researchers have identified a novel serum lectin from the lamprey, termed LSSL (Lamprey Serum Spherical Lectin). This study provides deep insights into the structural and functional characteristics of LSSL, demonstrating its significant role in immune regulation and pathogen elimination. Using advanced techniques like cryogenic electron microscopy (cryo-EM), the researchers uncovered that LSSL contains two structural calcium ions essential for its glycan-binding activity.

LSSL was found to exhibit a high binding capacity to both microbial and mammalian glycans and agglutination activity against bacteria. Phylogenetic analysis suggested an interesting evolutionary history for LSSL, likely integrated into the lamprey genome via horizontal gene transfer from phage transposons. Functionally, LSSL’s association with mannose-binding lectin-associated serine protease 1 (MASP-1) and the subsequent deposition of the C3 fragment on target cells highlights its crucial role in immune responses.

Role and Application of the 100-Glycan Array

The 100-glycan array played an indispensable role in this research. This comprehensive array, featuring a wide range of glycan structures, was used to assess LSSL’s binding specificity. The study revealed that LSSL binds to various glycans, including Galβ1-3GlcNAc, GlcNAcβ1-2Man, Manα1-2Man, and Neu5Ac. This high-throughput screening allowed precise quantification of binding interactions through fluorescence intensity measurements.

LSSL (8 µg/mL) binding to 100 glycan microarray. Data are presented as the mean ± SDs; (n = 3 technical replicates). The images are reproduced from Lu, J. et al. A novel serum spherical lectin from lamprey reveals a more efficient mechanism of immune initiation and regulation in jawless vertebrates. Cell. Mol. Biol. Lett. 27, (2022).

By using the 100-glycan array, researchers could determine LSSL’s broad-spectrum glycan-binding capability, which is crucial for its immune recognition functions. The detailed binding profiles provided by the array facilitated a deeper understanding of LSSL’s mechanism of action. The findings demonstrate the utility of the 100-glycan array in glycan-protein interaction studies, making it an invaluable tool for the scientific community. This technology can accelerate discoveries in immunology, particularly in understanding pathogen recognition and immune response mechanisms. Researchers can leverage the 100-glycan array (now CatchAll Glycan Array) to explore various glycan-binding proteins.