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  • 1
    Electronic Resource
    Electronic Resource
    Viral glycoproteins as determinants of pathogenicity (1982)
    Springer
    Medical microbiology and immunology 170 (1982), S. 145-153 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF02298195
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  • 2
    Electronic Resource
    Electronic Resource
    Induction of T cell response by bluetongue virus core-like particles expressing a T cell epitope of the M1 protein of influenza A virus (1998)
    Springer
    Medical microbiology and immunology 187 (1998), S. 91-96 
    Details
    ISSN: 1432-1831
    Keywords: Key words T cell epitopes ; Bluetongue virus ; Core-like particles ; Influenza virus M1 protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A CD4+ T cell epitope of the influenza virus matrix protein corresponding to the C terminus (QAYQKRMGVQMQRFK) was inserted into the VP7 gene of bluetongue virus (BTV). The chimeric protein was expressed by a dual recombinant Autographa californica polyhedrosis virus (AcNPV), which encodes the two inner capsid proteins VP3 and VP7 of BTV. When Spodoptera frugiperda cells (Sf9 cells) were infected with this recombinant BTV, core-like particles (CLPs) were formed as demonstrated by electron microscopy. To study the immunogenicity of a foreign epitope deprived of its natural flanking sequences in vitro, purified CLPs expressing the T cell epitope were used to stimulate two different MHC class II-restricted CD4+ human T cell clones. One of these T cell clones, ALF 3.7 was specific for the inserted epitope, whereas the other T cell clone ALF 4.4 recognized shorter derivates of the given epitope. CLPs with the inserted epitope were presented as efficiently as purified influenza virus matrix protein to the clone ALF 3.7, whereas clone ALF 4.4 showed no proliferative response.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004300050078
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  • 3
    Electronic Resource
    Electronic Resource
    Early molecular events during the interaction of enveloped riboviruses with cells (1979)
    Springer
    European biophysics journal 5 (1979), S. 25-32 
    Details
    ISSN: 1432-1017
    Keywords: DPH-migration ; Virus adsorption ; Virus penetration ; Cells membranes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract A kinetic model was constructed and partly solved to describe the migration of the fluorescence label 1,6-diphenylhexatriene (DPH) in both directions when enveloped viruses, labelled with DPH in their envelopes are in contact with unlabelled cells or cell labelled in their membranes are in contact with unlabelled enveloped viruses. The central assumption is that two types of receptor sites exist on the cell surface, i.e., physical adsorption sites (P-sites), available to all the viruses studied in these papers and binding sites (B-sites) available only to the viruses which penetrate into the specific cells. The differential equations for the label migration, for different values of the ratio number of viruses number of sites were numerically solved, assuming different fractions of P- and B-sites. The equations also describe, appropriately the mechanism of rapid label migration in the system and substantiate the magnitude “time of residence” of the nonpenetrating viruses adsorbed on the cell surface. The resulting curves match satisfactorily those for the label release by the viruses and account well for the steady state values of the kinetics of label migration in the virus-cell system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00535770
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  • 4
    Electronic Resource
    Electronic Resource
    Early molecular events in the interaction of enveloped viruses with cells (1979)
    Springer
    European biophysics journal 5 (1979), S. 11-23 
    Details
    ISSN: 1432-1017
    Keywords: Fluorescence polarization degree ; Fusion ; Label migration ; Lipid migration ; Cell membrane ; Virus envelope
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract The fluorescence depolarization of 1,6-diphenyl-hexatriene was used to study the dynamic properties of the hydrophobic regions of the lipid envelopes of ortho- and paramyxoviruses as well as of the Rous sarcoma virus and of the membrane lipids of susceptible and nonsusceptible cells. The systems investigated where active and inactive influenza viruses, and NDV virus acting on chick embryo fibroblasts and Rous sarcoma virus acting on susceptible (C/E) and nonsusceptible (C/B) chicken-cell. Polarization degrees and mean rotational correlation times of DPH embedded in viral lipids were significantly higher than those of DPH in the cell membranes, due to a higher rigidity of the virus envelopes. When suspensions of labelled viruses and unlabelled cells or unlabelled viruses and labelled cells were mixed, a characteristic change of the fluorescence polarization degrees with time was observed. This behaviour was ascribed to a label transfer from virus to cell membranes or vice versa. While the rate constants of label transfer from virus to cells and cells to virus were about the same for the penetrating viruses the rate constants of label release from inactive virus to cells were much larger than for the migration in the opposite direction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00535769
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  • 5
    Electronic Resource
    Electronic Resource
    Molecular events during the interaction of envelopes of myxo- and RNA-tumor viruses with cell membranes. A 270 MHz ^1H nuclear magnetic resonance study
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 511 (1978), S. 83-92 
    Details
    ISSN: 0005-2736
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0005-2736(78)90066-4
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  • 6
    Electronic Resource
    Electronic Resource
    Methyl α-glycoside of N-thioacetyl-d-neuraminic acid: A potential inhibitor of influenza A virus a ^1H NMR study
    Amsterdam : Elsevier
    FEBS Letters 334 (1993), S. 117-120 
    Details
    ISSN: 0014-5793
    Keywords: Binding affinity ; Hemagglutinin ; Influenza A virus ; ^1H NMR ; α-2-O-Methyl-N-thioacetylneuraminic acid
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(93)81694-U
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  • 7
    Electronic Resource
    Electronic Resource
    Strain-specific differences in the effect of influenza A virus neuraminidase on vector-expressed hemagglutinin (1999)
    Springer
    Archives of virology 144 (1999), S. 781-786 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary.  In order to evaluate the efficiency of the removal of sialic acid residues from the influenza virus hemagglutinin by the viral neuraminidase in the course of the virus replication cycle, CV-1 cells expressing the hemagglutinin of H7 subtype from an SV40-based vector were superinfected with influenza virus strain A/Duck/Ukraine/63 (H3N8) or A/USSR/90/77 (H1N1). Vector-expressed hemagglutinin was immunoprecipitated from cell lysates and analyzed by polyacrylamide gel electrophoresis. The data indicate that the removal of sialic acid residues from the vector-expressed H7 hemagglutinin by N1 neuraminidase of A/USSR/90/77 virus in the course of the virus replication cycle is incomplete. The results are discussed in connection with previously published data showing that the low activity of NA in wild-type influenza virus results in incomplete removal of sialic acid residues from virion components.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007050050543
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  • 8
    Electronic Resource
    Electronic Resource
    Biological functions of monospecific antibodies to envelope glycoproteins of Newcastle disease virus (1984)
    Springer
    Archives of virology 81 (1984), S. 53-65 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Monospecific antisera to HN and F glycoproteins of Newcastle disease virus were prepared, and their effects on the biological activities of the virus were investigated. Anti-HN serum inhibited hemagglutinating and neuraminidase activity, as well as hemolysis. Anti-F serum had no effect on hemagglutination or neuraminidase but inhibited hemolysis and virus-induced cell fusion. Anti-HN serum was highly neutralizing, while neutralization by anti-F serum was very inefficient in conventional plaque reduction tests, although both sera were estimated to contain comparable amounts of antibody reacting with the virus as indicated by complement fixation and immunodiffusion tests. The neutralizing activity of anti-F serum was greatly enhanced by the addition of anti-IgG serum or fresh guinea pig serum, whereas that of anti-HN serum was little enhanced. Anti-HN serum incorporated in the agar overlay suppressed the development of plaques to some degree, while anti-F serum had little effect. The combination of anti-HN and anti-F sera resulted in a marked decrease in the number and size of plaques, demonstrating the synergistic effect of the two species of antibody in the containment of the spread of viral infection.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01309296
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  • 9
    Electronic Resource
    Electronic Resource
    Significance of basolateral domain of polarized MDCK cells for Sendai virus-induced cell fusion (1992)
    Springer
    Archives of virology 125 (1992), S. 129-139 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Fusion (fusion from within) of polarized MDCK monolayer cells grown on porous membranes was examined after infection with Sendai viruses. Wild-type virus, that buds at the apical membrane domain, did not induce cell fusion even when the F glycoprotein expressed at the apical domain was activated with trypsin. On the other hand, a protease activation mutant, F 1-R, with F protein in the activated form and that buds bipolarly at the apical and basolateral domains, caused syncytia formation in the absence of exogenous protease. Anti-Sendai virus antibodies added to the basolateral side, but not at the apical side, inhibited cell fusion induced by F 1-R. In addition, T-9, a mutant with bipolar budding phenotype of F 1-R but with an uncleavable F protein phenotype like wild-type virus, induced cell fusion exclusively when trypsin was added to the basolateral medium. By electron microscopy, cell-to-cell fusion was shown to occur at the lateral domain of the plasma membrane. These results indicate that in addition to proteolytic activation of the F protein, basolateral expression of Sendai virus envelope glycoproteins is required to induce cell fusion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01309633
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  • 10
    Electronic Resource
    Electronic Resource
    The carbohydrates of influenza virus (1978)
    Springer
    Archives of virology 56 (1978), S. 251-255 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Two carbohydrate fractions can be obtained from egg-grown influenza virus after Pronase digestion followed by gel chromatography. One fraction contains glycopeptides (MW ca. 2000–2600) which represent the carbohydrate side chains of the viral glycoproteins. The constituent sugars of this material are fucose, galactose, glucosamine, and mannose, and their position within the side chain has been partially elucidated by methylation studies. The other fraction (MW〉6000) appears to be mucopolysaccharide and is composed of fucose, galactose, glucose, galactosamine, and glucosamine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01317854
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