A new kind of carbohydrate array, its use for profiling antiglycan antibodies, and the discovery of a novel human cellulose-binding antibody

TLDR

The study uses a novel glycan array to profile glycan‑binding antibodies in purified IgG from healthy humans and proposes it for high‑throughput screening and biomarker discovery. The array consists of mono‑ and oligosaccharides covalently attached through long linkers at their reducing ends, presenting them in a defined orientation for specific antibody binding. The array revealed a novel anticellulose antibody that preferentially binds β4‑linked glucopyranose over galactopyranose, as well as known antiglycan antibodies against bacterial polysaccharide components.

Abstract

In this study, we use a novel glycan array to analyze the glycan-binding antibody repertoire in a pool of affinity-purified IgG collected from a healthy human population. The glycan array used is based on mono- and oligosaccharides covalently linked to the surface via a long linker at their reducing ends. They are thus presented to the medium with a well-defined orientation and are accessible for specific binding by glycan-binding proteins, such as antibodies and lectins. A novel anticellulose antibody was detected that binds specifically to β4-linked saccharides with a preference for glucopyranose over galactopyranose residues. We also found previously known antiglycan antibodies against mono- and oligosaccharides that are constituents of commonly occurring bacterial polysaccharides. We propose that this array can facilitate high-throughput screening of glycan-binding proteins and the search for biomarkers for personalized medicine.