Search Results - (Author, Cooperation:H. D. Klenk)
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1Latest Papers from Table of Contents or Articles in PressR. A. Fouchier ; A. Garcia-Sastre ; Y. Kawaoka ; W. S. Barclay ; N. M. Bouvier ; I. H. Brown ; I. Capua ; H. Chen ; R. W. Compans ; R. B. Couch ; N. J. Cox ; P. C. Doherty ; R. O. Donis ; H. Feldmann ; Y. Guan ; J. Katz ; H. D. Klenk ; G. Kobinger ; J. Liu ; X. Liu ; A. Lowen ; T. C. Mettenleiter ; A. D. Osterhaus ; P. Palese ; J. S. Peiris ; D. R. Perez ; J. A. Richt ; S. Schultz-Cherry ; J. Steel ; K. Subbarao ; D. E. Swayne ; T. Takimoto ; M. Tashiro ; J. K. Taubenberger ; P. G. Thomas ; R. A. Tripp ; T. M. Tumpey ; R. J. Webby ; R. G. Webster
American Association for the Advancement of Science (AAAS)
Published 2012Staff ViewPublication Date: 2012-01-28Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Animals ; *Biomedical Research ; Disease Models, Animal ; Ferrets ; Humans ; *Influenza A Virus, H5N1 Subtype/pathogenicity ; Influenza, Human/transmission/virology ; Orthomyxoviridae Infections/*transmission/virologyPublished by: -
2Latest Papers from Table of Contents or Articles in PressR. A. Fouchier ; A. Garcia-Sastre ; Y. Kawaoka ; W. S. Barclay ; N. M. Bouvier ; I. H. Brown ; I. Capua ; H. Chen ; R. W. Compans ; R. B. Couch ; N. J. Cox ; P. C. Doherty ; R. O. Donis ; H. Feldmann ; Y. Guan ; J. M. Katz ; O. I. Kiselev ; H. D. Klenk ; G. Kobinger ; J. Liu ; X. Liu ; A. Lowen ; T. C. Mettenleiter ; A. D. Osterhaus ; P. Palese ; J. S. Peiris ; D. R. Perez ; J. A. Richt ; S. Schultz-Cherry ; J. Steel ; K. Subbarao ; D. E. Swayne ; T. Takimoto ; M. Tashiro ; J. K. Taubenberger ; P. G. Thomas ; R. A. Tripp ; T. M. Tumpey ; R. J. Webby ; R. G. Webster
American Association for the Advancement of Science (AAAS)
Published 2013Staff ViewPublication Date: 2013-01-25Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Animals ; Biomedical Research/*trends ; Birds ; Humans ; *Influenza A Virus, H5N1 Subtype ; Influenza in Birds/*transmission/*virology ; Influenza, Human/*transmission/*virologyPublished by: -
3Latest Papers from Table of Contents or Articles in PressStaff View
Publication Date: 2015-08-15Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Animals ; Ebola Vaccines/*administration & dosage ; Ebolavirus/*immunology ; Glycoproteins/*immunology ; Hemorrhagic Fever, Ebola/*prevention & control ; Viral Proteins/*immunologyPublished by: -
4Articles: DFG German National LicensesGarn, H ; Wegmann, M ; Wagner, R ; Klenk, H-D ; Stech, J
[s.l.] : Nature Publishing Group
Published 2005Staff ViewISSN: 1546-170XSource: Nature Archives 1869 - 2009Topics: BiologyMedicineNotes: [Auszug] A promising approach to reduce the impact of influenza is the use of an attenuated, live virus as a vaccine. Using reverse genetics, we generated a mutant of strain A/WSN/33 with a modified cleavage site within its hemagglutinin, which depends on proteolytic activation by elastase. Unlike the ...Type of Medium: Electronic ResourceURL: -
5Articles: DFG German National LicensesTashiro, M. ; Ciborowski, P. ; Klenk, H.-D. ; Pulverer, G. ; Rott, R.
[s.l.] : Nature Publishing Group
Published 1987Staff ViewISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] In a host cell where an appropriate protease for post-translational proteolytic cleavage of the precursor haemag-glutinin (HA) of influenza virus into the HAX and HA2 fragments is not present and as a consequence infectious virus cannot be produced, infectivity can be recovered by in vitro ...Type of Medium: Electronic ResourceURL: -
6Articles: DFG German National LicensesStaff View
ISSN: 0005-2736Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyMedicinePhysicsType of Medium: Electronic ResourceURL: -
7Articles: DFG German National LicensesMachytka, D. ; Kharitonenkov, I. ; Isecke, R. ; Hetterich, P. ; Brossmer, R. ; Klein, R.A. ; Klenk, H.-D. ; Egge, H.
Amsterdam : ElsevierStaff ViewISSN: 0014-5793Keywords: Binding affinity ; Hemagglutinin ; Influenza A virus ; ^1H NMR ; α-2-O-Methyl-N-thioacetylneuraminic acidSource: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002Topics: BiologyChemistry and PharmacologyPhysicsType of Medium: Electronic ResourceURL: -
8Articles: DFG German National LicensesNicolau, C. ; Klenk, H. -D. ; Hildenbrand, K. ; Reimann, B. ; Reimann, Alice ; Bauer, H.
Springer
Published 1979Staff ViewISSN: 1432-1017Keywords: Fluorescence polarization degree ; Fusion ; Label migration ; Lipid migration ; Cell membrane ; Virus envelopeSource: Springer Online Journal Archives 1860-2000Topics: BiologyPhysicsNotes: 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 ResourceURL: -
9Articles: DFG German National LicensesStaff View
ISSN: 1432-1017Keywords: DPH-migration ; Virus adsorption ; Virus penetration ; Cells membranesSource: Springer Online Journal Archives 1860-2000Topics: BiologyPhysicsNotes: 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 ResourceURL: -
10Articles: DFG German National LicensesTashiro, M. ; Yamakawa, M. ; Tobita, K. ; Klenk, H. -D. ; Seto, J. T. ; Rott, R.
Springer
Published 1992Staff ViewISSN: 1432-8798Source: Springer Online Journal Archives 1860-2000Topics: MedicineNotes: 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 ResourceURL: -
11Articles: DFG German National LicensesStaff View
ISSN: 1432-8798Source: Springer Online Journal Archives 1860-2000Topics: MedicineNotes: 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 ResourceURL: -
12Articles: DFG German National LicensesUmino, Y. ; Kohama, T. ; Kohase, M. ; Sugiura, A. ; Klenk, H. -D. ; Rott, R.
Springer
Published 1987Staff ViewISSN: 1432-8798Source: Springer Online Journal Archives 1860-2000Topics: MedicineNotes: Summary The protective effect of humoral immunity against lethal infection of chickens with Newcastle disease virus was studied. Chickens hatched from eggs laid by hens vaccinated with live attenuated Newcastle disease virus vaccine possessed antibody to various components of the virus, and were resistant to a challenge with a virulent strain of Newcastle disease virus which was 100 per cent fatal for the offspring of nonvaccinated hens. Passive administration of antiserum raised against whole virions provided susceptible chickens protection comparable to that seen in the birds with maternal antibody. When administered passively, both anti-HN serum with virus neutralizing activity, and anti-F serum with only marginal virus neutralizing activity significantly prolonged the survival of infected birds but failed to achieve the level of protection as afforded by the anti-whole NDV serum. The protection provided by the simultaneous presence of anti-HN and anti-F serum was significantly greater than that afforded by either alone and comparable to that of anti-whole NDV serum, indicating the complementary effect of anti-HN and anti-F antibodies not only in cell cultures as reported previously (19), but also in a natural host.Type of Medium: Electronic ResourceURL: -
13Articles: DFG German National LicensesStaff View
ISSN: 1432-8798Source: Springer Online Journal Archives 1860-2000Topics: MedicineNotes: Summary The numbers of the carbohydrate side chains have been analyzed on a series of subtype 7 hemagglutinins of influenza A virus. The procedure employed involves growth of the virus in the presence of the trimming inhibitor N-methyl-1-desoxynojirimycin followed by controlled removal of the resulting mannose-rich oligosaccharides with endo-N-acetylglucosaminidase H. By comparative analysis with virus grown in the absence of the inhibitor oligomannosidic side chains can be discriminated from complex ones. The results show that all H7 hemagglutinins have a complex and an oligomannosidic side chain on HA2, whereas the oligosaccharides of HA1 vary in number.Type of Medium: Electronic ResourceURL: -
14Articles: DFG German National LicensesStaff View
ISSN: 1432-8798Source: Springer Online Journal Archives 1860-2000Topics: MedicineNotes: Summary The acetylesterase of influenza C virus has been reported recently to be inhibited by diisopropylfluorophosphate (DFP) [Muchmore EA, Varki A (1987) Science 236: 1293–1295]. As this inhibitor is known to bind covalently to the serine in the active site of serine esterases, we attempted to determine the serine in the active site of the influenza C acetylesterase. Incubation of purified influenza C virus with3H-DFP resulted in the selective labelling of the influenza C glycoprotein HEF. The labelled glycoprotein was isolated from a SDS-polyacrylamide gel. Following reduction and carboxymethylation, tryptic peptides of HEF were prepared and analyzed by reversed phase HPLC. The peptide containing the3H-DFP was subjected to sequence analysis. The amino acids determined from the NH2-terminus were used to locate the peptide on the HEF polypeptide. Radiosequencing revealed that3H-DFP is attached to amino acid 17 of the tryptic peptide. These results indicate that serine 71 is the active-site serine of the acetylesterase of influenza C virus.Type of Medium: Electronic ResourceURL: -
15Articles: DFG German National LicensesStaff View
ISSN: 1432-8798Source: Springer Online Journal Archives 1860-2000Topics: MedicineNotes: 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 ResourceURL: -
16Articles: DFG German National LicensesBiological functions of monospecific antibodies to envelope glycoproteins of Newcastle disease virusUmino, Y. ; Kohama, T. ; Kohase, M. ; Sugiura, A. ; Klenk, H. -D. ; Rott, R.
Springer
Published 1984Staff ViewISSN: 1432-8798Source: Springer Online Journal Archives 1860-2000Topics: MedicineNotes: 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 ResourceURL: -
17Articles: DFG German National LicensesStaff View
ISSN: 1432-8798Source: Springer Online Journal Archives 1860-2000Topics: MedicineNotes: Summary Analysis of the effects of amantadine during a single cycle of replication of A/FPV/Rostock virus in vitro showed that, as with other influenza A viruses, an M 2 protein-dependent step early in infection was inhibited. No effect was observed on later steps in replication under the conditions used.Type of Medium: Electronic ResourceURL: -
18Articles: DFG German National LicensesSeidel, W. ; Künkel, F. ; Geisler, B. ; Garten, W. ; Herrmann, B. ; Döhner, L. ; Klenk, H. -D.
Springer
Published 1991Staff ViewISSN: 1432-8798Source: Springer Online Journal Archives 1860-2000Topics: MedicineNotes: 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 ResourceURL: -
19Articles: DFG German National LicensesOkada, H. ; Seto, J. T. ; McQueen, N. L. ; Klenk, H.-D. ; Rott, R. ; Tashiro, M.
Springer
Published 1998Staff ViewISSN: 1432-8798Source: Springer Online Journal Archives 1860-2000Topics: MedicineNotes: Summary. Mutations in the fusion, F, protein of Sendai virus resulting in increased cleavability by ubiquitous host protease(s), and mutations in the matrix, M, protein resulting in bipolar budding, are both important determinants for the systemic infection in mice caused by the protease activating pantropic mutant, F1-R. Several mutants of Sendai virus (BY, BF, and KD-M) with phenotypes of bipolar budding and/or increased cleavability of F protein were isolated. Genomic RNA sequence analysis of the F and M genes of the mutants revealed that several deduced amino acids in the F and M proteins were different from those of F1-R, T-5 (a revertant of F1-R), and wild-type viruses. The BF and KD-M mutants that budded bipolarly and were also activated by ubiquitous proteases were examined for replication in tissue culture cells and in mice. All of the mutants exhibited multiple-step replication in MDCK, MDBK, and LLC-MK2 cells without trypsin, but formed plaques only in MDCK cells. One of the mutants, designated KD-52M, was similar to F1-R in that it formed plaques in all three cell lines without addition of exogenous protease. However, none of the mutant viruses, including KD-52M, caused a systemic infection in mice. The mutated M protein of F1-R enhances the disruption of microtubles. However, none of the mutants with a bipolar budding phenotype (BY, BF, and KD-M), disrupted the microtubules to the same extent as F1-R. All of these mutants had mutations in the M protein that were different from those found in F1-R. Taken together, these results suggest that mutations at Ser115 to Pro in the F protein and at Asp 128 to Gly and Ile210 to Thr in the M protein of F1-R are the mutations specifically required for the systemic infection caused by F1-R.Type of Medium: Electronic ResourceURL: -
20Articles: DFG German National LicensesStaff View
ISSN: 1432-8798Source: Springer Online Journal Archives 1860-2000Topics: MedicineNotes: Summary The spread of infection in the chorioallantoic membrane (CAM) has been analysed with pathogenic and non-pathogenic avian influenza A viruses. After allantoic inoculation of pathogenic strains, high titers of infectious virus were found in the allantoic fluid, and virus growth could be demonstrated by immunohistology and electron microscopy in the allantoic epithelium, the mesenchyma, and in the chorionic epithelium. By the same route of inoculation, non-pathogenic strains yielded also high titers of infectious virus in the allantoic fluid, but virus replication was restricted to the allantoic epithelium and did not occur in the other cell layers. After chorionic inoculation of pathogenic strains, replication occurred in all layers of the CAM, and infectious virus was released into the allantoic fluid. However, when the chorionic epithelium was infected with a non-pathogenic strain, infection did not spread beyond the site of inoculation. These differences in virus spread are based on differential activation of the hemagglutinin by proteolytic cleavage. The hemagglutinin of pathogenic strains is cleaved in cells of each layer, whereas the hemagglutinin of non-pathogenic strains is cleaved only in the allantoic epithelium. In epithelial cells, virus budding occurred nearly exclusively at the apical side of the cell surface, but this polarization of virus maturation was found with both pathogenic and nonpathogenic strains, indicating that it does not account for the differences in virus spread and, thus, in pathogenicity.Type of Medium: Electronic ResourceURL: