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  • 1990-1994  (1)
  • 1980-1984  (2)
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  • 1990-1994  (1)
  • 1980-1984  (2)
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  • 1
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Cultured cells of the chorioallantoic membrane (CAM) fulfilled the need of using the same cell system that was permissive for representative paramyxoviruses to carry out studies on the biosynthesis of their glycoproteins in infected cells. The polypeptide composition of the respective paramyxoviruses [Newcastle disease virus (NDV), paramyxovirus Yucapipa (PMY), and Sendai virus], grown in eggs and CAM-cells, was essentially identical. In egg-grown PMY a large glycoprotein (LGP) was present but only in some CAM-grown preparations of virus labeled with [3H]-glucosamine and rarely in [35S]-methionine or [3H]-amino acids (valine, leucine, and tyrosine) labeled viruses. The site of cleavage of precursor F0 to F1,2 was not the same. In contrast to the cleavage of Sendai virus glycoprotein, cleavage was intracellular in NDV and PMY infected cells. Homologous antisera against the glycoproteins failed to inhibit cleavage of HN0 or F0 in cells infected with the representative paramyxoviruses.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary During the epidemic outbreak in the region of Greifswald in the winter 1974/75, we found influenza virus variants which showed differences in the electrophoretic mobility of HA. Among the 25 isolates 13 were of slower and 12 of higher mobility. HA1 of 6 isolates was studied by determining the number of the carbohydrate side chains and by direct sequencing of vRNA. Evidence is presented that variants showing a slower electrophoretic mobility of HA1 had consistently acquired a seventh carbohydrate side chain at Asn 126 in epitope A. All the isolates differed from the reference strain A/Port Chalmers/1/73 by the loss of the oligosaccharide at Asn 81. The field strain A/Dresden/3/71 possessed only 5 oligosaccharides in HA1. These results suggest that changes in glycosylation are an important mechanism in the structural variation underlying antigenic drift of HA.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Medical microbiology and immunology 170 (1982), S. 145-153 
    ISSN: 1432-1831
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Conclusion With myxoviruses we are now beginning to understand the complex biological phenomenon of pathogenicity at the molecular level. Proteolytic activation of the viral glycoproteins proved to be a very important determinant for pathogenicity. Variations in pathogenicity are the result of structural variations of the glycoproteins. The available evidence indicates that these structural variations are confined to the cleavage site, i.e., to a small but functionally important part of the molecule.
    Type of Medium: Electronic Resource
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