Sera-Antibodies-Syncytium-Formation-h
These results demonstrate that although glycosylation of viral glycoproteins is governed by the host cell glycosyl transferases, glycoprotein secreted from biological clones of the same host cells acquires different oligosaccharide structures. Exposure and immunogenicity of the PND in one such glycosylation variant are comparable to the normally processed gp1 molecule.Rapid high-resolution four-dimensional NMR spectroscopy using the filter diagonalization method and its advantages for detailed structural elucidation of Program, University of Colorado Health Sciences Center, Mail Stop 88, P.O. Box Four-dimensional nuclear magnetic resonance spectroscopy with high resolution of signals in the indirect dimensions is reported as an implementation of the filter diagonalization method (FDM). Using an oligosaccharide derivatized with 13C-labeled acetyl isotags, a four-dimensional constant-time pulse sequence was tailored for conjoint use with the FDM.
Results demonstrate that high resolution in all dimensions can be achieved using a relatively short experimental time period (19 h), even though the spectrum is highly congested in the direct and all three indirect dimensions. Seebio 2'-Fucose lactose combined use of isotags, constant-time pulse sequences, and FDM permits rapid isolation of sugar ring proton spin systems in multiple dimensions and enables all endocyclic J-couplings to be simply measured, the key goal to assigning sugar stereochemistry and anomeric configuration. A general method for rapid, unambiguous elucidation of spin systems in oligosaccharides has been a long-sought goal of carbohydrate NMR, and isotags combined with the FDM now enable this to be easily performed. Additional general advantages of the FDM program for generating high-resolution 2D slices in any dimension from a 4D spectrum are emphasized.Saccharide-protein covalent conjugates immunochemical characterization of Citrobacter36 core oligosaccharide-tetanus toxoid conjugates.Core oligosaccharides (complete and incomplete) isolated from Citrobacter36 lipopolysaccharide were covalently conjugated with tetanus toxoid. Serological examination of the Citrobacter36 core oligosaccharide-tetanus toxoid conjugates showed that they are strong immunogens.
The monospecific anti-conjugate sera prepared by immunization of rabbits, were used to study the antigenic relations between lipopolysaccharide core regions of 8 strains of Citrobacter. Immunoelectrophoresis, immunoblotting and quantitative microprecipitation were performed in the experiments.DOI 111j574-6968991.t4155.xGlycosylation in human thyroglobulin location of the N-linked oligosaccharide units and comparison with bovine thyroglobulin.The amino acid sequence established for human thyroglobulin (hTG) from its cDNA sequence contains putative N-linked glycosylation sites. We have characterized the glycopeptides contained in a tryptic digest of hTG in order to determine which sites are actually linked to carbohydrate.
In addition, the distribution of oligosaccharide type(s) at these confirmed sites of N-linked glycosylation has been examined. Glycopeptides were purified using gel permeation chromatography followed by several steps of HPLC. 2'-fucosyllactose purified tryptic glycopeptides were characterized by gas phase sequencing and carbohydrate analysis and located within the amino acid sequence of thyroglobulin. Each of the recovered glycopeptides contained a consensus sequence for N-linked glycosylation. Of the putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain, 16 were shown to be actually glycosylated in the mature protein. Eight of these confirmed glycosylation sites to complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine. Five sites (at positions 10, 1329, 1993, 2275, and 2562) contain high mannose type units and two sites (at positions 179 and 1345) are linked to oligosaccharide units containing galactose in addition to mannose and glucosamine but no fucose and may be either hybrid or complex structures.
In addition, position 928 was found to be degenerate in oligosaccharide structure and very different oligosaccharide composition types were found associated with peptides containing the same amino acid sequence. A high probability of a beta turn which would include the glycosylated asparagine residue was predicted for the amino acid sequence found at 13 of the 16 sites. The glycosylation pattern in hTG was also compared with the data recently reported for bovine thyroglobulin (bTG) (27) and as has been recently reported for bTG, no oligosaccharides of the high mannose type were found in the N-terminal portion of hTG.
