Interaction of Viruses, Bacteria and Bacterial Toxins with Host Cell Surface Glycolipids. Aspects on Receptor Identification and Dissection of Binding Epitopes

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Abstract
Specific attachment of viruses and bacteria to carbohydrate has long been known, although it is only recently that the subject is being treated more extensively. The work of Burnet and co-workers in the 1940’s revealed an enzyme activity, “receptor destroying enzyme”, RDE, responsible for specific inhibition of influenza virus binding to cell surfaces.1 Later, Faillard in Klenk’s laboratory identified the substance being split off as NeuAc.2 At about the same time it was shown that several bacte specifically recognized Man.3 About 15 years after, van Heyningen and co-workers opened up4 an intense period of studies on the NecAc containing glycolipid, the ganglioside GM1, as a specific receptor for cholera toxin.5 Concerning glycolipid receptors**, Haywood demonstrated6 a specific binding of Sendai virus to liposomes containing brain gangliosides. Since then, its specificity and biological relevance have been further investigated.7, 8 More recently, two independent groups9, 10 demonstrated a specific binding of E. coli to Galα1→4Gal- containing glycolipids causing urinary tract infection of man. This result was the impetus for a more systematic study of glycolipids as receptors for viruses and bacteria as is now being performed in our laboratory. Recent reviews summarize the receptor knowledge in the case of viruses,11 bacteria12 and bacterial toxins.5