Host-mediated selection of influenza virus receptor variants. Sialic acid-alpha 2,6Gal-specific clones of A/duck/Ukraine/1/63 revert to sialic acid-alpha 2,3Gal-specific wild type in ovo.

摘要: Human and animal influenza A isolates of the H3 serotype preferentially bind SA alpha 2,6Gal or 2,3Gal linkages (where represents sialic acid), respectively, on cell-surface sialyloligosaccharides. Previously, we have demonstrated selection 2,3Gal-specific receptor variants several human viruses which differed from parent by a single amino acid at residue 226 hemagglutinin is located in binding pocket (Rogers, G. N., Paulson, J.C., Daniels, R.S., Skehel, J.J., Wilson, I.A., Wiley, D.C. (1983) Nature 304, 76-78). In this report, reverse direction was accomplished starting with avian virus, A/duck/Ukraine/1/63 (H3N7), yielding 2,6Gal-specific that exhibit properties characteristic isolates. Selection again mediated hemagglutinin, case changing Gln virus to Leu variants. Although were stable passage MDCK cells, they exhibited dramatic reversion phenotype during chicken embryos. This contrast both hosts. The eggs provides compelling evidence for host-mediated