measles/carbohydrate

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The glycoprotein of measles virus. External radioactive labelling of its carbohydrate and partial characterization of the glycopeptide.

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Measles virus was propagated in VERO cells and purified from the culture supernatants by two successive tartrate-density-gradient centrifugations. Surface carbohydrates were labelled both in vitro and in vivo with 3H after treatment with galactose oxidase/NaB3H4 or with [3H]glucosamine. The major

Adherence of human peripheral blood lymphocytes to measles-virus infected cells: modulation by solubilized rhesus erythrocyte membranes and carbohydrates.

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The adherence of human peripheral blood lymphocytes to HeLa cells persistently infected with measles virus (HeLa-K11) was studied. The following data were observed. (i) The proportion of HeLa-K11 cells with adherent human peripheral blood lymphocytes of rhesus monkey erythrocytes was similar over a

[Effect of measles on carbohydrate metabolism].

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Purification of measles virus by affinity chromatography and by ultracentrifugation: a comparative study.

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The purification of viruses by ultracentrifugation in regions with limited resources is often hampered by problems of instrument maintenance. Viral antigens must therefore be imported, which results in delays in obtaining epidemiological data. To address this problem, we undertook the development of

Influence of N-linked oligosaccharide chains on the processing, cell surface expression and function of the measles virus fusion protein.

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The fusion (F) glycoprotein of measles virus, a structural component of the virion envelope, contains four potential sites for attachment of N-linked oligosaccharides. Three are located in the F2 subunit of the protein and one in the signal peptide. Four mutants were constructed by

Probing the spatial organization of measles virus fusion complexes.

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The spatial organization of metastable paramyxovirus fusion (F) and attachment glycoprotein hetero-oligomers is largely unknown. To further elucidate the organization of functional fusion complexes of measles virus (MeV), an archetype of the paramyxovirus family, we subjected central predictions of

Analysis of structural proteins of measles, canine distemper, and rinderpest viruses.

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Serological relationships among measles virus (MV), canine distemper virus (CDV), and rinderpest virus (RV), which constitute morbillivirus subgroup of paramyxoviridae, were investigated by immunoprecipitation and SDS-polyacrylamide gel electrophoresis for their major structural proteins, i.e.,

Membrane cofactor protein with different types of N-glycans can serve as measles virus receptor.

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Membrane cofactor protein (MCP) has been shown to act as a cellular receptor for measles virus. In previous binding studies we demonstrated a direct interaction between the measles virus H protein and MCP. The binding was shown to be independent of the O-glycans but dependent on the N-glycans of

Molecular characterization of epitopes on the measles virus hemagglutinin protein.

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The measles virus (MV) hemagglutinin (H) gene nucleotide sequences of the LEC-WI strain and 11 branched sequential neutralization escape variants of the strain derived by selection with five monoclonal antibodies (Mabs) were determined by direct analysis of amplified polymerase chain reaction

Maturation of measles virus hemagglutinin glycoprotein.

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The processing of measles virus hemagglutinin glycoprotein (H) in infected cells was studied by pulse-chase method and two-dimensional isoelectric focusing and SDS-polyacrylamide slab gel electrophoresis. H glycoprotein was synthesized initially as polypeptides smaller than H glycoprotein present in

Antiviral and immunostimulating effects of lignin-carbohydrate-protein complexes from Pimpinella anisum.

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Three antiviral and immunostimulating substances (LC1, LC2 and LC3) were isolated from a hot water extract of seeds of Pimpinella anisum by combination of anion-exchange, gel filtration and hydrophobic interaction column chromatographies. Chemical and spectroscopic analyses revealed them to be

Expression of ABO or related antigenic carbohydrates on viral envelopes leads to neutralization in the presence of serum containing specific natural antibodies and complement.

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No definitive biologic function has been associated with the human ABO histo-blood group polymorphism, or any other terminal carbohydrate differences within or between closely related species. We have experimentally addressed the question of whether viral particles can become glycosylated as

Role of N-linked oligosaccharide chains in the processing and antigenicity of measles virus haemagglutinin protein.

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The effects of N-linked oligosaccharides on the haemagglutinin (H) protein of measles virus (MV) were assessed with respect to the processing and antigenicity of the molecule. The functional glycosylation sites on the H protein were determined by eliminating each of the five potential positions,

Mononuclear leukocytes preferentially bind via CD44 to hyaluronan on human intestinal mucosal smooth muscle cells after virus infection or treatment with poly(I.C).

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Pathological changes in inflammatory bowel disease include an increase in intestinal mucosal mononuclear leukocytes and hyperplasia of the muscularis mucosae smooth muscle cells (M-SMCs). Because virus infections have correlated with disease flare, we tested the response of cultured M-SMCs to

Genetically modified viruses: vaccines by design.

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Vaccination has been one of the most successful and cost-effective health interventions ever employed. One disease (smallpox) has been eradicated, another (poliomyelitis) should disappear early in the new millennium and a third (measles) should follow shortly after. Conventional vaccines usually

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