Interaction of viruses, bacteria and bacterial toxins with host cell surface glycolipids. Aspects on receptor identification and dissection of binding epitopes.

An overview and perspective is presented on animal cell surface carbohydrate (primarily lipid-linked oligosaccharides) as specific receptors for viruses, bacteria and bacterial toxins. Although carbohydrate has been known for many years to be specific attachment sites for these ligands, it is only in very recent time that carbohydrate technology and receptor assays in combination afford a rational approach. One generalization from present experience is the property of microbiological ligands to recognize sequences placed internally in an oligosaccharide chain which differs from antibody recognition of short sequences which most often involves terminally placed determinants. This is of both biological and technical importance. Biologically it may assure attachment by avoiding differences between host individuals often residing in terminal parts (e.g. blood group determinants), and may also make a shift of target cells by mutations more efficient. Technically this property is an important help when dissecting narrow binding epitopes, and for disclosing receptor-binding variants with only slight differences in binding epitopes (e.g. different epitopes on the same disaccharide). Such variants representing a kind of "epitope drift" are probably a consequence of point mutations in the binding site of the lectin-like proteins to select a proper host environment. Current technology allows an efficient screening for carbohydrate receptors with interesting consequences for applications within medicine (diagnosis and therapy) and biotechnology.