On the Structure of the Oligosaccharides in Glycoprotein 71 (Gp71) From Friend Leukemia Virus (Flv)

Geyer, Rudolf; Geyer, Hildegard; Hunsmann, G; Schneider, Josef; Stirm, Stephan

doi:10.1042/bst009145pc

Cited by 3 publications

(11 citation statements)

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“…Newcastle-disease virus was generously given by Dr. H. D. Klenk (University of Marburg, Marburg, Germany). The structure and origin of oligosaccharide standards used for chromatographic comparison and calibration were given in detail previously [20]. Glucose oligoners with 1-25 glucose units were prepared by partial hydrolysis of dextran as described by Yamashita et al [22].…”

Section: Materials and Methods Materialsmentioning

confidence: 99%

“…Virus-infected cells were maintained in RPMI-1640 medium (Selectamine; Gibco, Eggenstein, Germany) containing 10% (v/v) fetal-bovine serum and 2 mM-glutamine. For metabolic labelling, 4.5 x 107 cells in the exponential growth phase were 'starved' for 30 min in glucose-free medium, then incubated with 5 mCi of D- [6-3H]glucosamine hydrochloride (33 mCi/mmol; Amersham, Braunschweig, Germany) for 2 h in glucose-free medium, for 4 h in glucose-deficient medium (0.13 mg of glucose/ml) and for another 20 h in normal RPMI medium [20]. After centrifugation, radiolabelled glycoprotein was isolated from the cell-free supernatant by indirect immunoprecipitation using a cross-reacting high-titred serum of a naturally infected African green monkey (Cercopithecus aethiops) and Protein A-Sepharose CL-4B beads (Pharmacia, Uppsala, Sweden) [10,23,24].…”

Section: Preparation Of Radiolabelied Sivsm Gpl30mentioning

confidence: 99%

“…After desalting, radiolabelled sialic acids were identified by h.p.l.c. on an Aminex HPX-87H column [20,26]. For the release of neutral and amino-sugar components, the acetone precipitate was further hydrolysed with 500 #1 of 250 mM-H2SO4 in aq.…”

Section: Identification Of Radiolabelled Monosaccharidesmentioning

confidence: 99%

“…Isolation and fractionation of oligosaccharides Proteolytic digestion of gpl.30, release of radiolabelled sugar side chains by treatment with endo-fl-N-acetylglucosaminidase H (endo H) and peptide: N-glycosidase F (PNGase F), separation of oligosaccharides from residual (glyco)peptides by gel filtration or reversed-phase h.p.l.c., reduction of oligosaccharides as well as fractionation of oligosaccharide alditols by h.p.l.c. using columns of LiChrosorb Diol, LiChrosorb NH2 (Merck, Darmstadt, Germany) or Mikropak AX-5 (Varian, Walnut Creek, CA, U.S.A.) and desalting of oligosaccharide alditols were carried out as described previously [20,26].…”

Section: Identification Of Radiolabelled Monosaccharidesmentioning

confidence: 99%

“…In a previous study [20] we have, therefore, analysed the structures of the oligosaccharide side chains of gpl20 from HIV-1 propagated in the human T-cell line H9. Here we describe the characterization of the oligosaccharide species attached to gpl 30 from SIVSM' an isolate from sooty mangabey (Cercocebus atys) [21].…”

Section: Introductionmentioning

confidence: 99%

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Glycosylation of the envelope glycoprotein gp130 of simian immunodeficiency virus from sooty mangabey (Cercocebus atys)

Holschbach¹,

Schneider

Geyer³

1990

Biochemical Journal

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The envelope glycoprotein 130 ('130' referring to an Mr of 130,000) of simian immunodeficiency virus from sooty mangabey (Cercocebus atys) (SIVSM) was isolated from the cell-free supernatant of the SIVSM-infected human T-cell line H9, metabolically labelled with D-[6-3H]glucosamine. After digestion with Staphylococcus aureus V8 proteinase, radiolabelled N-glycans were liberated from resulting glycopeptides by sequential treatment with endo-beta-N-acetylglucosaminidase H and peptide:N-glycosidase F and fractionated by h.p.l.c. and gel filtration. Individual oligosaccharide species were characterized by enzymic microsequencing, chromatographic analyses and, in part, by acetolysis. The oligosaccharide structures thus established include oligomannosidic glycans with five to nine mannose residues as well as fucosylated and partially sialylated bi-, tri- and tetra-antennary N-acetyl-lactosaminic oligosaccharide species, the latter of which carry, in part, additional galactose residues or N-acetyl-lactosamine repeats. In comparison with the corresponding envelope glycoprotein 120 from human immunodeficiency virus type 1 (HIV-1), propagated in the same cell line [Geyer, Holschbach, Hunsmann and Schneider (1988) J. Biol. Chem. 263, 11760-11767], carbohydrates of the simian glycoprotein were found to consist of decreased amounts of oligomannosidic glycans and increased quantities of higher-branched N-acetyl-lactosaminic species.

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Section: Materials and Methods Materialsmentioning

confidence: 99%

Section: Preparation Of Radiolabelied Sivsm Gpl30mentioning

confidence: 99%

Section: Identification Of Radiolabelled Monosaccharidesmentioning

confidence: 99%

Section: Identification Of Radiolabelled Monosaccharidesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Glycosylation of the envelope glycoprotein gp130 of simian immunodeficiency virus from sooty mangabey (Cercocebus atys)

Holschbach¹,

Schneider

Geyer³

1990

Biochemical Journal

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Interaction of mannose-binding lectin with primary isolates of human immunodeficiency virus type 1

Saifuddin

Hart

Gewürz

et al. 2000

Journal of General Virology

133

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Complex-type N-linked oligosaccharides of gp120 from human immunodeficiency virus type 1 contain sulfated N-acetylglucosamine

Shilatifard

Merkle

Helland

et al. 1993

J Virol

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The major envelope glycoproteins gpl20 and gp4l of human immunodeficiency virus type 1, the causative agent for human AIDS, contain numerous N-linked oligosaccharides. We report here our discovery that N-acetylglucosamine residues within the complex-type N-linked oligosaccharides of both gpl20 and its precursor, gpl60, are sulfated. When human Molt-3 ceUs persistently infected with human T-cell leukemia virus IIB were metabolicall radiolabeled with 3-SO4 gpl60, gpl20, and to some extent gp4l were radiolabeled. The 35SO4-labeled oligosaccharides were quantitatively released by N-glycanase treatment and were bound by immobilized Ricinus communis agglutinin I, a lectin that binds to terminal ,3-galactosyl residues. The kinetics of release of sulfate upon acid hydrolysis from 35S04-labeled gpl20 indicate that sulfation occurs in a primary sulfate ester linkage. Methylation analysis of total glycopeptides from Molt-3 cells metabolically radiolabeled with [3H]glucosamine demonstrates that sulfation occurs at the C-6 position of N-acetylglucosamine. Fragmentation of the gpl20-derived 35S04-labeled glycopeptides by treatment with hydrazine and nitrous acid and subsequent reduction generated galactosyl-anhydromannitol-6-35504, which is the expected reaction product from GlcNAc-6-sulfate within a sulfated lactosamine moiety. Charge analysis of the [3H]galactoseand [3H]glucosamine-labeled glycopeptides from gpl20 and gpl60 indicates that approximately 14% of the complex-type N-linked oligosaccharides are sulfated.

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On the Structure of the Oligosaccharides in Glycoprotein 71 (Gp71) From Friend Leukemia Virus (Flv)

Cited by 3 publications

References 0 publications

Glycosylation of the envelope glycoprotein gp130 of simian immunodeficiency virus from sooty mangabey (Cercocebus atys)

Glycosylation of the envelope glycoprotein gp130 of simian immunodeficiency virus from sooty mangabey (Cercocebus atys)

Interaction of mannose-binding lectin with primary isolates of human immunodeficiency virus type 1

Complex-type N-linked oligosaccharides of gp120 from human immunodeficiency virus type 1 contain sulfated N-acetylglucosamine

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