Search results for "Glycoprotein"

ChemInform Abstract: Synthesis of Glycopeptide Partial Structures of Virus Coat Glycoproteins

2010

Description of a Simple, Specific, and Sensitive Test for the Detection of Detergent-Solubilized C3b Receptor

1981

Abstract The C3b receptor was isolated from detergent-solubilized human erythrocyte membranes by a previously described technique (1). The receptor glycoprotein was shown to enhance EAC14oxy23b rosette formation with Raji lymphoblastoid cells. This provided a specific and sensitive test to detect the solubilized C3b receptor either in crude or highly purified form. The property of the C3b receptor tested by this assay appears to be analogous to properties of β1H.

Self-assembly properties of the proteinaceous coat secreted by the ?slime? variant of Neurospora crassa

1989

The proteinaceous extracellular material (PEM) synthesized by the cells of the ‘slime” strain of Neurospora crassa (see Martinez et al. 1989) was solubilized by treatment with urea or guanidine. Removal of these chemicals by dialysis, caused reassembly of the solubilized proteins into material with the same microscopic appearance as the original PEM. Polypeptide patterns from both native and reassembled structures were identical. Dialysis-mediated reassembly of the solubilized proteins appeared to be dependent on both concentration of the soluble macromolecules and time. Gel chromatography of PEM solubilized with different agents revealed two discrete populations of complexes with molecular…

Large-scale analysis of SARS-CoV-2 spike-glycoprotein mutants demonstrates the need for continuous screening of virus isolates

2021

AbstractDue to the widespread of the COVID-19 pandemic, the SARS-CoV-2 genome is evolving in diverse human populations. Several studies already reported different strains and an increase in the mutation rate. Particularly, mutations in SARS-CoV-2 spike-glycoprotein are of great interest as it mediates infection in human and recently approved mRNA vaccines are designed to induce immune responses against it.We analyzed 146,917 SARS-CoV-2 genome assemblies and 2,393 NGS datasets from GISAID, NCBI Virus and NCBI SRA archives focusing on non-synonymous mutations in the spike protein.Only around 13.8% of the samples contained the wild-type spike protein with no variation from the reference. Among…

Hemocyanin from the keyhole limpetMegathura crenulata(KLH) carries a novel type of N-glycans with Gal(β1-6)Man-motifs

2002

Keyhole limpet (Megathura crenulata) hemocyanin (KLH), an extracellular respiratory protein, is widely used as hapten carrier and immune stimulant. Although it is generally accepted that the sugar constituents of this glycoprotein are likely to be implicated in the antigenicity and biomedical properties of KLH, knowledge of its carbohydrate structure is still limited. Therefore, we have investigated the N-linked oligosaccharides of KLH. Glycan chains were enzymatically liberated from tryptic glycopeptides, pyridylaminated and separated by two-dimensional HPLC. Only neutral oligosaccharides were obtained and characterized by carbohydrate constituent and methylation analyses, MALDI-TOF-MS, ES…

Synthesis of Azido-Glycans for Chemical Glycomodification of Proteins

2018

Role of glycosylation in the incorporation of intrinsic mannoproteins into cell walls of Saccharomyces cerevisiae.

1989

Cell wall mannoproteins from Saccharomyces cerevisiae are completely or partially incorporated into their final location when N-glycosylation is inhibited by tunicamycin. These include a 90–100 kDa species still containing O-linked oligomannose chains, derived from a N-glycosylated material larger than 120 kDa; and a 30.5 kDa peptide lacking mannose residues, derived from a 33 kDa species. For both species, the growth temperature influences the level of incorporation of the non N-glycosylated molecules. Secretion of the peptides lacking N-linked saccharide chains follows the route defined by sec mutants.

Sulfated and Non-Sulfated Glycopeptide Recognition Domains of P-Selectin Glycoprotein Ligand 1 and their Binding to P- and E-Selectin

2009

Total synthesis through block glycosylation and selective chemical O-sulfation of tyrosine residues yielded the glycopeptide recognition domain A (X=SO(3) (-)) of the P-selectin glycoprotein ligand 1, in which the terminal sialic acid of the complex hexasaccharide side chain was replaced by (S)-cyclohexyl lactic acid. In binding assays the O-sulfated structure A showed high affinity towards P-selectin, the non-sulfated towards E-selectin.

Loss of Contact-Dependent Inhibition of Growth in Chemically Transformed Fibroblasts

1988

The plasma membrane has been recognized as an important regulatory unit of mammalian cells during determination, differentiation, and social behaviour of individual cells within various tissues (1–4). On the molecular level, plasma membrane glycoproteins and glycolipids have been shown to be involved in these processes (1–4). Density-dependent growth of non-transformed cells in vitro has been proposed to be regulated by secreted inhibitory compounds (5–7), by the cell’s shape (8) or by diffusion boundary layers (9). On the other hand, specific cell-cell interactions via cell membrane molecules were found to be of great importance for the contact-dependent inhibition of growth (10–16) and co…

Antitumor Vaccines Based on Synthetic Mucin Glycopeptides

2011

The interest in tumor-associated glycoconjugate antigens was particularly initiated by Springer, who published in 1984 that glycoproteins on the outer cell-membrane of epithelial tumor cells have an altered glycosylation consisting of the Thomsen-Friedenreich (T-) antigen and its precursor the TN-antigen structure (Springer 1984). He and his coworkers also had found that monoclonal antibodies induced with glycoproteins from tumor cell membranes showed cross-reactivity to desialylated glycophorin A. It was concluded from these observations that the T-and TN-glycoproteins on the epithelial tumor cells must be structurally related to asialoglycophorin A (Springer et al. 1983) (Fig. 11.1a). Gly…