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• W1610339662 abstract "Research Article1 October 1985free access Carbohydrates of influenza virus. Structural elucidation of the individual glycans of the FPV hemagglutinin by two-dimensional 1H n.m.r. and methylation analysis. W. Keil W. Keil Search for more papers by this author R. Geyer R. Geyer Search for more papers by this author J. Dabrowski J. Dabrowski Search for more papers by this author U. Dabrowski U. Dabrowski Search for more papers by this author H. Niemann H. Niemann Search for more papers by this author S. Stirm S. Stirm Search for more papers by this author H.D. Klenk H.D. Klenk Search for more papers by this author W. Keil W. Keil Search for more papers by this author R. Geyer R. Geyer Search for more papers by this author J. Dabrowski J. Dabrowski Search for more papers by this author U. Dabrowski U. Dabrowski Search for more papers by this author H. Niemann H. Niemann Search for more papers by this author S. Stirm S. Stirm Search for more papers by this author H.D. Klenk H.D. Klenk Search for more papers by this author Author Information W. Keil, R. Geyer, J. Dabrowski, U. Dabrowski, H. Niemann, S. Stirm and H.D. Klenk The EMBO Journal (1985)4:2711-2720https://doi.org/10.1002/j.1460-2075.1985.tb03991.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info The structures of the oligosaccharides of the hemagglutinin of fowl plague virus [influenza A/FPV/Rostock/34 (H7N1)] have been elucidated by one- and two-dimensional 1H n.m.r. spectroscopy at 500 MHz and by microscale methylation analysis. N-Glycosidic oligosaccharides of the oligomannosidic (OM) and of the N-acetyllactosaminic type have been found, the latter type comprising biantennary structures, without (A) or with (E) bisecting N-acetylglucosamine, and triantennary (C) structures. Analysis of the tryptic and thermolytic glycopeptides of the hemagglutinin allowed the allocation of these oligosaccharides to the individual glycosylation sites. Each attachment site contained a unique set of oligosaccharides. Asn12 contains predominantly structures C and E which are highly fucosylated. Asn28 contains OM and A structures that lack fucose and sulfate. Asn123 shows A that has incomplete antennae but is highly fucosylated and sulfated. Asn149 has fucosylated A and E. Asn231 shows fucosylated A and E with incomplete antennae. Asn406 has OM oligosaccharides. Asn478 has A and E with little fucose. Localization of the oligosaccharides on the three-dimensional structure of the hemagglutinin revealed that the oligomannosidic glycans are attached to glycosylation sites at which the enzymes responsible for carbohydrate processing do not have proper access. These observations demonstrate that an important structural determinant for the oligosaccharide side chains is the structure of the glycoprotein itself. In addition, evidence was obtained that the rate of glycoprotein synthesis also has an influence on carbohydrate structure. Next ArticlePrevious Article Volume 4Issue 101 October 1985In this issue RelatedDetailsLoading ..." @default.
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• W1610339662 title "Carbohydrates of influenza virus. Structural elucidation of the individual glycans of the FPV hemagglutinin by two-dimensional 1H n.m.r. and methylation analysis." @default.
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