Diversity of sugar chain recognition by hemagglutinin and transmission mechanism of influenza viruses

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This project aims at explicating the role of hemagglutinin on the replication of influenza viruses and transmission of the viruses between the hosts.The results of the project are as follows.1. We tested the binding reactivity of human H3 influenza A viruses, which were isolated from 1968 to 1979, to sialylglycolipids containing different molecular species of terminal sialic acids. All human H3 viruses tested bound both Neu5Ac and Neu5Gc.2. We examined the relative abundance of Neu5Ac and Neu5Gc in the epithelial cells of horse trachea. More than 90 % of the sialic acid was Neu5Gc, while the remaining proportion was NeuAc. The major sialic acid-Galactose moiety present in horse tracheal epithelial cells is Neu5Gcα2.3Gal. We examined the requirement for the hemagglutinin for support of viral replication in horses, using viruses whose Has differ in receptor specificity. The results indicated that recognition of Neu5Gcα2,3Gal moiety is critical for viral replication in horses.3. The recognition of a glycoconjugate moiety possessing Neu5Gcα2,3Gal was associated with viral replication in duck intestine.4. Sulfatide binding site is localized in the sialic acid binding pocket of HA or the neighborhood of the pocket.