Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Sulfation of the N-linked oligosaccharides of influenza virus hemagglutinin: temporal relationships and localization of sulfotransferases
Autore:
Spiro, NJ; Spiro, RG;
Indirizzi:
Harvard Univ, Sch Med, Joslin Diabet Ctr, Elliot P Joslin Res Lab, Boston,MA 02215 USA Harvard Univ Boston MA USA 02215 ot P Joslin Res Lab, Boston,MA 02215 USA Harvard Univ, Sch Med, Dept Med, Boston, MA 02215 USA Harvard Univ BostonMA USA 02215 Sch Med, Dept Med, Boston, MA 02215 USA Harvard Univ, Sch Med, Dept Biol Chem, Boston, MA 02215 USA Harvard Univ Boston MA USA 02215 ed, Dept Biol Chem, Boston, MA 02215 USA
Titolo Testata:
GLYCOBIOLOGY
fascicolo: 11, volume: 10, anno: 2000,
pagine: 1235 - 1242
SICI:
0959-6658(200011)10:11<1235:SOTNOO>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANS-GOLGI NETWORK; COMPLEX CARBOHYDRATE UNITS; D-GALACTOSYL RESIDUES; BREFELDIN-A; MDCK CELLS; STRUCTURAL ELUCIDATION; KIDNEY-CELLS; RAT-LIVER; GLYCOPROTEINS; PROTEINS;
Keywords:
sulfated N-linked oligosaccharides; influenza virus hemagglutinin; sulfotransferases; subcellular localization; glycoprotein processing sequence;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Spiro, RG Harvard Univ, Sch Med, Joslin Diabet Ctr, Elliot P Joslin Res Lab, 1 Joslin Pl, Boston, MA 02215 USA Harvard Univ 1 Joslin Pl Boston MA USA02215 oston, MA 02215 USA
Citazione:
N.J. Spiro e R.G. Spiro, "Sulfation of the N-linked oligosaccharides of influenza virus hemagglutinin: temporal relationships and localization of sulfotransferases", GLYCOBIOLOG, 10(11), 2000, pp. 1235-1242

Abstract

The occurrence of sulfate substituents on several positions of glycoprotein N-linked oligosaccharides prompted us to determine the subcellular localization and temporal relationships of the addition of these anionic groups employing as a model system the hemagglutinin (HA) produced by influenza virus-infected Madin-Darby canine kidney (MDCK) cells. It became apparent froma study of the HA glycoprotein in subcellular fractions resolved by Nycodenz gradient centrifugation following pulse-chase radiolabeling that sulfation of the complex N-linked oligosaccharides occurs only after they have been processed to an endo-beta -N-acetylglucosaminidase-resistant state and have reached the medial/trans Golgi and the trans Golgi network (TGN), with the former carrying out most of the sulfation activity. Hydrazine/nitrous acid/NaBH4 treatment of the HA from the subcellular fractions indicated that C-3 of the galactose as well as C-6 of the N-acetylglucosamine residues of the N-acetyllactosamine chains became sulfated in these post ER fractions, as did the C-6 of the outer N-acetylglucosamine of the di-N-acetylchitobiose core. Consistent with the specificities of the stepwise assembly of the N-acetyllactosamine branches, we observed that the 3'-phosphoadenosine 5'-phosphosulfate (PAPS):GlcNAc-6-O-sulfotransferase migrated in the gradient toa medial/trans Golgi position while in contrast the PAPS:Gal-3-O-sulfotransferase was found in both Golgi and TGN locations. In accordance with the concept that beta -galactosylation must precede the sulfation catalyzed by the latter enzyme, we observed the presence of UDP-Gal:GlcNAc galactosyltransferase in both these sites in the MDCK cells. The presence of the Gal-3-O-sulfotransferase in the TGN is particularly important in the influenza virus-infected cells, as it makes possible the addition of terminal anionic groups after removal of the sialic acid residues by the viral neuraminidase.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 06:58:02