BIOMAT Database Logo BIOMAT Database Logo

Oligosaccharides at individual glycosylation sites in glycoprotein 71 of Friend murine leukemia virus. 1990

R Geyer, and J Dabrowski, and U Dabrowski, and D Linder, and M Schlüter, and H H Schott, and S Stirm
Biochemisches Institut am Klinikum der Justus-Liebig-Universitat, Giessen, Federal Republic of Germany.

Glycoprotein 71 from Friend murine leukemia virus was digested with proteases and the glycopeptides obtained were isolated and assigned, by amino acid sequencing, to the eight N-glycosylated asparagines in the molecule; only Asn334 and Asn341 could not be separated. The oligosaccharides liberated from each glycopeptide by endo-beta-N-acetylglucosaminidase H, or by peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F, were fractionated and subjected to structural analysis by one- and two-dimensional 1H NMR, as well as by methylation/gas-liquid-chromatography/mass-fragmentography. At each glycosylation site, the substituents were found to be heterogeneous including, at Asn334/341 and Asn410, substitution by different classes of N-glycans: oligomannosidic oligosaccharides, mainly Man alpha 1----6(Man alpha 1----3)Man alpha 1----6(Man alpha 1----3)Man beta 1----4GlcNAc beta 1----4GlcNAc beta 1----, were detected at Asn168, Asn334/341 and Asn410. Hybrid species, partially sialylated, intersected and (proximally) funcosylated Man alpha 1----6(Man alpha 1----3)Man alpha 1----6 and Man alpha 1----3Man alpha 1----6 and Man alpha 1----3Man alpha 1----6(Gal beta 1----4GlcNAc beta 1----2Man alpha 1----3)Man beta 1----4GlcNAc beta 1----4GlcNAc beta 1----, were found at Asn12, as previously published [Schlüter, M., Linder, D., Geyer, R., Hunsmann, H., Schneider, J. & Stirm, S. (1984) FEBS Lett. 169, 194-198] and at Asn334/341. N-Acetyllactosaminic glycans, mainly partially intersected and fucosylated NeuAc alpha 2----3 or Gal alpha 1----3Gal beta 1----4GlcNAc beta 1----2Man alpha 1----6(NeuAc alpha 2----6 or NeuAc alpha 2----3Gal-beta 1----4GlcNAc beta 1----2Man alpha 1----3)Man beta 1----4GlcNac beta 1----4GlcNAc beta 1---- with some bifurcation at ----6Man alpha 1----6, were obtained from Asn266, Asn302, Asn334/341, Asn374 and Asn410. In addition, Thr268, Thr277, Thr279, Thr304/309, as well as Ser273 and Ser275, were found to be O-glycosidically substituted by Gal beta 1----3GalNAc alpha 1----, monosialylated or desialylated at position 3 of Gal or/and position 6 of GalNAc.

UI MeSH Term Description Entries
D008745 Methylation Addition of methyl groups. In histo-chemistry methylation is used to esterify carboxyl groups and remove sulfate groups by treating tissue sections with hot methanol in the presence of hydrochloric acid. (From Stedman, 25th ed) Methylations
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009682 Magnetic Resonance Spectroscopy Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING). In Vivo NMR Spectroscopy,MR Spectroscopy,Magnetic Resonance,NMR Spectroscopy,NMR Spectroscopy, In Vivo,Nuclear Magnetic Resonance,Spectroscopy, Magnetic Resonance,Spectroscopy, NMR,Spectroscopy, Nuclear Magnetic Resonance,Magnetic Resonance Spectroscopies,Magnetic Resonance, Nuclear,NMR Spectroscopies,Resonance Spectroscopy, Magnetic,Resonance, Magnetic,Resonance, Nuclear Magnetic,Spectroscopies, NMR,Spectroscopy, MR
D009844 Oligosaccharides Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form. Oligosaccharide
D010449 Peptide Mapping Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases. Fingerprints, Peptide,Peptide Fingerprinting,Protein Fingerprinting,Fingerprints, Protein,Fingerprint, Peptide,Fingerprint, Protein,Fingerprinting, Peptide,Fingerprinting, Protein,Mapping, Peptide,Peptide Fingerprint,Peptide Fingerprints,Protein Fingerprint,Protein Fingerprints
D002236 Carbohydrate Conformation The characteristic 3-dimensional shape of a carbohydrate. Carbohydrate Linkage,Carbohydrate Conformations,Carbohydrate Linkages,Conformation, Carbohydrate,Conformations, Carbohydrate,Linkage, Carbohydrate,Linkages, Carbohydrate
D002240 Carbohydrate Sequence The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS. Carbohydrate Sequences,Sequence, Carbohydrate,Sequences, Carbohydrate
D005622 Friend murine leukemia virus A strain of Murine leukemia virus (LEUKEMIA VIRUS, MURINE) producing leukemia of the reticulum-cell type with massive infiltration of liver, spleen, and bone marrow. It infects DBA/2 and Swiss mice. Friend Virus,Rowson-Parr Virus,Rowson Parr Virus,Virus, Friend,Virus, Rowson-Parr
D006020 Glycopeptides Proteins which contain carbohydrate groups attached covalently to the polypeptide chain. The protein moiety is the predominant group with the carbohydrate making up only a small percentage of the total weight. Glycopeptide
D006031 Glycosylation The synthetic chemistry reaction or enzymatic reaction of adding carbohydrate or glycosyl groups. GLYCOSYLTRANSFERASES carry out the enzymatic glycosylation reactions. The spontaneous, non-enzymatic attachment of reducing sugars to free amino groups in proteins, lipids, or nucleic acids is called GLYCATION (see MAILLARD REACTION). Protein Glycosylation,Glycosylation, Protein

Related Publications

R Geyer, and J Dabrowski, and U Dabrowski, and D Linder, and M Schlüter, and H H Schott, and S Stirm
Isolation of glycopeptides containing individual glycosylation sites of Friend murine leukemia virus glycoprotein: studies of glycosylation by methylation analysis.
May 1985, Carbohydrate research,
R Geyer, and J Dabrowski, and U Dabrowski, and D Linder, and M Schlüter, and H H Schott, and S Stirm
The glycoprotein 71 of ecotropic Friend murine leukemia virus. Structure of the oligosaccharides linked to asparagine-12.
April 1984, FEBS letters,
R Geyer, and J Dabrowski, and U Dabrowski, and D Linder, and M Schlüter, and H H Schott, and S Stirm
Complete amino acid sequence and glycosylation sites of glycoprotein gp71A of Friend murine leukemia virus.
October 1982, Proceedings of the National Academy of Sciences of the United States of America,
R Geyer, and J Dabrowski, and U Dabrowski, and D Linder, and M Schlüter, and H H Schott, and S Stirm
Mutational analysis of N-linked glycosylation sites of Friend murine leukemia virus envelope protein.
October 1991, Journal of virology,
R Geyer, and J Dabrowski, and U Dabrowski, and D Linder, and M Schlüter, and H H Schott, and S Stirm
Separation procedure and sugar composition of oligosaccharides in the surface glycoprotein of Friend murine leukemia virus.
August 1982, Biochimica et biophysica acta,
R Geyer, and J Dabrowski, and U Dabrowski, and D Linder, and M Schlüter, and H H Schott, and S Stirm
Localization of the intrachain disulfide bonds of the envelope glycoprotein 71 from Friend murine leukemia virus.
January 1992, European journal of biochemistry,
R Geyer, and J Dabrowski, and U Dabrowski, and D Linder, and M Schlüter, and H H Schott, and S Stirm
The asparagine-linked oligosaccharides at individual glycosylation sites in human thyrotrophin.
October 1992, Glycobiology,
R Geyer, and J Dabrowski, and U Dabrowski, and D Linder, and M Schlüter, and H H Schott, and S Stirm
Host-dependent variation of asparagine-linked oligosaccharides at individual glycosylation sites of Sindbis virus glycoproteins.
February 1983, The Journal of biological chemistry,
R Geyer, and J Dabrowski, and U Dabrowski, and D Linder, and M Schlüter, and H H Schott, and S Stirm
Structure of the oligosaccharides sensitive to endo-beta-n-acetylglucosaminidase H in the glycoprotein of Friend murine leukemia virus.
September 1984, European journal of biochemistry,
R Geyer, and J Dabrowski, and U Dabrowski, and D Linder, and M Schlüter, and H H Schott, and S Stirm
Structural elements in glycoprotein 70 from polytropic Friend mink cell focus-inducing virus and glycoprotein 71 from ecotropic Friend murine leukemia virus, as defined by disulfide-bonding pattern and limited proteolysis.
August 1994, Journal of virology,
Copied contents to your clipboard!