Normal human plasma anti-beta-glucoside antibody has markedly elevated IgA content and binds fungal and yeast polysaccharides.

Normal human plasma antibody that recognizes beta-linked glucoside moiety was purified by affinity chromatography on cellulose. The anti-beta-glucoside antibody had three times higher IgA to IgG ratio and substantially higher polymeric IgA content than total serum immunoglobulins. Cellobiose and other beta-glucosides were best inhibitors of its binding to polystyrene microwell-coated polysaccharides. In synthetic glycoproteins made by conjugating disaccharides to hemoglobin or bovine serum albumin, cellobiose, unlike lactose or maltose, was sugar-specifically recognized by the antibody. It also recognized polystyrene well-coated beta1-->3 linked glycans of Saccharomyces cerevisiae, Candida albicans and of barley in decreasing order of affinity. Its sugar-binding site could thus accommodate beta-glucoside with or without substitution at C4 and C3. High IgA content along with the capacity to bind common microbial and dietary antigens pointed to the immune inflammatory potential of the antibody.