Thomssen, Reiner

[["dc.bibliographiccitation.firstpage","435"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Der Chirurg"],["dc.bibliographiccitation.lastpage","+"],["dc.bibliographiccitation.volume","73"],["dc.contributor.author","Thomssen, R."],["dc.date.accessioned","2018-11-07T10:30:05Z"],["dc.date.available","2018-11-07T10:30:05Z"],["dc.date.issued","2002"],["dc.identifier.doi","10.1007/s00104-002-0436-2"],["dc.identifier.isi","000175919000006"],["dc.identifier.pmid","12089826"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43785"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0009-4722"],["dc.title","Hepatitis B - The HBV-infected surgeon: an infection risk for the patient"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","177"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Medical Microbiology and Immunology"],["dc.bibliographiccitation.lastpage","184"],["dc.bibliographiccitation.volume","188"],["dc.contributor.author","Monazahian, M."],["dc.contributor.author","Kippenberger, S."],["dc.contributor.author","Mueller, A."],["dc.contributor.author","Seitz, H."],["dc.contributor.author","Bohme, I."],["dc.contributor.author","Grethe, S."],["dc.contributor.author","Thomssen, R."],["dc.date.accessioned","2018-11-07T10:48:52Z"],["dc.date.available","2018-11-07T10:48:52Z"],["dc.date.issued","2000"],["dc.description.abstract","Heterogeneities in the density of hepatitis C virus (HCV)-RNA-carrying material from human sera (1.03-1.20 g/ml) are partially due to the binding of lipoproteins [low density (LDL), very low density (VLDL), high density (HDL) lipoproteins] and immunoglobulins. In this study we demonstrate the binding of recombinant HCV envelope protein (E1/E2) to human LDL, VLDL and HDL on a molecular basis. The binding: of lipoproteins was restricted to the middle part of the El gene product (amino acids 222-336) and the C-terminal part of the E2 protein (amino acids 523-809). Lipoproteins did not bind to recombinant HCV core protein."],["dc.identifier.doi","10.1007/s004300000032"],["dc.identifier.isi","000088186500003"],["dc.identifier.pmid","10917154"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/48300"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0300-8584"],["dc.title","Binding of human lipoproteins (low, very low, high density lipoproteins) to recombinant envelope proteins of hepatitis C virus"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Virology"],["dc.bibliographiccitation.lastpage","7"],["dc.bibliographiccitation.volume","74"],["dc.contributor.author","Koschel, M."],["dc.contributor.author","Oed, D."],["dc.contributor.author","Gerelsaikhan, T."],["dc.contributor.author","Thomssen, R."],["dc.contributor.author","Bruss, V."],["dc.date.accessioned","2018-11-07T11:10:44Z"],["dc.date.available","2018-11-07T11:10:44Z"],["dc.date.issued","2000"],["dc.description.abstract","Recently we generated a panel of hepatitis B virus core gene mutants carrying single insertions or deletions which allowed efficient expression of the core protein in bacteria and self-assembly of capsids, Eleven of these mutations were introduced into a eukaryotic core gene expression vector and characterized by trans complementation of a core-negative HBV genome in cotransfected human hepatoma HuH7 cells. Surprisingly, four mutants (two insertions [EFGA downstream of All and LDTASALYR downstream of R39] and two deletions [Y38-R39-E40 and L42] produced no detectable capsids, The other seven mutants supported capsid formation and pregenome packaging/viral minus- and plus-strand-DNA synthesis but to different levels. Four of these seven mutants (two insertions [GA downstream of All and EHCSP downstream of P50] and two deletions [S44 and A80]) allowed virion morphogenesis and secretion. The mutant carrying a deletion of A80 at the tip of the spike protruding from the capsid was hepatitis B virus core antigen negative but wild type with respect to virion formation, indicating that this site might not be crucial for capsid-surface protein interactions during morphogenesis. The other three nucleocapsid-forming mutants tone insertion [LS downstream of S141] and two deletions [T12 and P134]) were strongly blocked in virion formation. The corresponding sites are located in the part of the protein forming the body of the capsid and not in the spike. These mutations may alter sites on the particle which contact surface proteins during envelopment, or they may block the appearance of a signal for the transport or the maturation of the capsid which is linked to viral DNA synthesis and required for envelopment."],["dc.identifier.isi","000084137100001"],["dc.identifier.pmid","10590084"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/53271"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","1098-5514"],["dc.relation.issn","0022-538X"],["dc.title","Hepatitis B virus core gene mutations which block nucleocapsid envelopment"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","29"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Medical Virology"],["dc.bibliographiccitation.lastpage","36"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Mihm, Sabine"],["dc.contributor.author","Monazahian, M."],["dc.contributor.author","Grethe, S."],["dc.contributor.author","Meier, V."],["dc.contributor.author","Thomssen, R."],["dc.contributor.author","Ramadori, Giuliano"],["dc.date.accessioned","2018-11-07T10:54:20Z"],["dc.date.available","2018-11-07T10:54:20Z"],["dc.date.issued","2000"],["dc.description.abstract","The hepatitis C virus (HCV) interferon-alpha (IFN-alpha) sensitivity-determining region (ISDR) has been shown to suppress double-stranded RNA-dependent protein kinase (PKR) activity in vitro in a yeast PKR expression system. Since variability of ISDR was shown to correlate with nonresponsiveness to IFN-alpha therapy in chronically HCV-infected patients, it has been suggested that prototype ISDR might be a viral inhibitor of cellular PKR. The present study evaluates the biological significance of ISDR variability in situ, relating it to PKR-mediated cellular antiviral responses within the liver. ISDR variability was determined in patients chronically infected with HCV genotypes 1a, 1b, and 3a by direct sequencing using liver-derived RNA preparations as starting material. As surrogate parameters for PKR-mediated cellular responses, hepatic endogenous IFN-alpha gene expression as well as MxA expression were analysed by a competitive, quantitative reverse transcription-polymerase chain reaction technique. Irrespectively of intra- or intergenotypic ISDR amino acid substitutions, ISDR variability was found not to correlate with endogenous hepatic IFN-alpha or with hepatic MxA gene expression. The data suggest that at least two prominent PKR-mediated cellular responses might be largely unaffected by HCV ISDR variability. J. Med. Virol. 61:29-36, 2000. (C) 2000 Wiley-Liss, Inc."],["dc.identifier.doi","10.1002/(SICI)1096-9071(200005)61:1<29::AID-JMV5>3.0.CO;2-C"],["dc.identifier.isi","000086206900005"],["dc.identifier.pmid","10745229"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/49542"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-liss"],["dc.relation.issn","0146-6615"],["dc.title","Lack of clinical evidence for involvement of hepatitis C virus interferon-alpha sensitivity-determining region variability in RNA-dependent protein kinase-mediated cellular antiviral responses"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","154"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","European Journal of Clinical Investigation"],["dc.bibliographiccitation.lastpage","155"],["dc.bibliographiccitation.volume","31"],["dc.contributor.author","Schettler, Volker"],["dc.contributor.author","Monazahian, M."],["dc.contributor.author","Wieland, Eberhard"],["dc.contributor.author","Ramadori, Giuliano"],["dc.contributor.author","Grunewald, Rolf W."],["dc.contributor.author","Thomssen, R."],["dc.contributor.author","Mueller, Gerhard A."],["dc.date.accessioned","2018-11-07T09:23:53Z"],["dc.date.available","2018-11-07T09:23:53Z"],["dc.date.issued","2001"],["dc.description.abstract","Background The association of HCV with apolipoprotein B containing lipoproteins has been observed and this led to the assumption that the LDL receptor may also serve as a candidate receptor for HCV. H.E.L.P.-LDL apheresis is suggested to be an effective and rapid tool to safely eliminate apolipoprotein B containing lipoproteins. Materials and methods In this pilot study, we have investigated whether H.E.L.P. treatment would reduce HCV load in five patients, all infected for more than 4 years with HCV and resistant against established anti-HCV therapy (interferon, ribaverin). HCV-RNA was determined by RT-PCR in plasma immediately before the start of apheresis (SA) and after treatment of 2500 mL plasma (AA). Results H.E.L.P. apheresis led to a mean decrease of 77.3% (16th percentile 36.5%, 84 th percentile 89.6%) of HCV-RNA when AA values were compared to SA values. This decline was reproducible during nine treatment procedures, but was not correlated to the decrease in LDL cholesterol. Conclusions This investigation shows for the first time that HCV load can be reduced by H.E.L.P. apheresis, which is an established and approved therapy for hypercholesterolemia. Even though the efficiency of viral load reduction varied between single procedures and did not correlate to LDL removal, this extracorporeal therapy opens the possibility to treat patients with established immune modulatory and antiviral therapy in the interval between two apheresis procedures."],["dc.identifier.doi","10.1046/j.1365-2362.2001.00758.x"],["dc.identifier.isi","000167703900011"],["dc.identifier.pmid","11168454"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29690"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Science Ltd"],["dc.relation.issn","0014-2972"],["dc.title","Reduction of hepatitis C virus load by HELP-LDL apheresis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","17"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Medical Microbiology and Immunology"],["dc.bibliographiccitation.lastpage","24"],["dc.bibliographiccitation.volume","191"],["dc.contributor.author","Thomssen, R."],["dc.contributor.author","Bonk, S."],["dc.date.accessioned","2018-11-07T10:30:21Z"],["dc.date.available","2018-11-07T10:30:21Z"],["dc.date.issued","2002"],["dc.description.abstract","In most sera of hepatitis C virus (HCV)infected patients beta-lipoproteins are bound to HCV RNA-carrying material, most often simultaneously with immunoglobulins (IgG, IgM) and sometimes additionally with high-density lipoproteins, forming complexes of low density (1.04-1.06 g/ml). To separate HCV particles from bound material, we tried to destroy the lipoprotein enzymatically by incubating HCV-positive human sera with lipoprotein lipase derived from Pseudomonas spp. (LPL-Ps). After this treatment, titers of HCV RNA in human sera (determined by a simple semiquantitative reverse transcription-PCR assay) were strongly reduced, regardless of whether primers of the NTR or NS5 region were used. Inactivation of HCV RNA could be inhibited by the addition of RNAguard to the serum-enzyme mixture. The lytic effect of the LPL-Ps preparation could be inhibited by tetrahydrolipstatin. Hence LPL-Ps seems to disrupt the HCV particle structure, including the putative core of the virus, and makes HCV RNA sensitive for RNase present in the reaction mixture. HBV was not destroyed by LPL-Ps. Porcine pancreatic lipase had no effect on HCV. The implications of these observations for the structure and biology of HCV and for its stability and inactivation in human sera are discussed."],["dc.identifier.doi","10.1007/s00430-001-0106-x"],["dc.identifier.isi","000176327500004"],["dc.identifier.pmid","12137195"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43851"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0300-8584"],["dc.title","Virolytic action of lipoprotein lipase on hepatitis C virus in human sera"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","152"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Medical Virology"],["dc.bibliographiccitation.lastpage","158"],["dc.bibliographiccitation.volume","60"],["dc.contributor.author","Grethe, S."],["dc.contributor.author","Gemsa, F."],["dc.contributor.author","Monazahian, M."],["dc.contributor.author","Bohme, I."],["dc.contributor.author","Uy, Angela"],["dc.contributor.author","Thomssen, R."],["dc.date.accessioned","2018-11-07T10:36:39Z"],["dc.date.available","2018-11-07T10:36:39Z"],["dc.date.issued","2000"],["dc.description.abstract","Infection with hepatitis C virus (HCV) is still a serious problem in hemodialysis patients, despite screening of blood products for anti-HCV antibodies. The prevalence of HCV in HD patients is between 15% and 30% in Germany. We report the molecular epidemiology of an HCV outbreak in a hemodialysis unit in 1997 is determined. HCV hypervariable region 1 (HVR1) was amplified from serum samples of 19 patients by polymerase chain reaction (PCR) and sequenced directly. In addition, HCV isolates from 3 of these 19 patients were cloned and sequenced. 14 newly infected patients and two patients, who had been infected for several years had very closely related HCV isolates. Unrelated HCV isolates as well as sequences obtained from an HCV outbreak in a plasmapheresis center were found in different, distantly related branches. These findings provide strong evidence for nosocomial transmission of the virus, despite following strict general hygiene precautions. The production of anti-HCV antibody was delayed significantly or seroconversion did not occur at all during the period of: observation in 8 out of 14 newly infected HCV RNA positive patients. Close-meshed reverse transcription-polymerase chain reaction (RT-PCR) analyses on apparently non infected patients within hemodialysis units and upon admission of new patients is strongly recommended for the early detection and prevention of outbreaks of HCV. J. Med. Virol, 60:152-158, 2000. (C) 2000 Wiley-Liss, Inc."],["dc.identifier.doi","10.1002/(SICI)1096-9071(200002)60:2<152::AID-JMV8>3.0.CO;2-I"],["dc.identifier.isi","000084428300008"],["dc.identifier.pmid","10596014"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/45380"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-liss"],["dc.relation.issn","0146-6615"],["dc.title","Molecular epidemiology of an outbreak of HCV in a hemodialysis unit: Direct sequencing of HCV-HVR1 as an appropriate tool for phylogenetic analysis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1004"],["dc.bibliographiccitation.issue","11-12"],["dc.bibliographiccitation.journal","Zeitschrift für Naturforschung C"],["dc.bibliographiccitation.lastpage","1010"],["dc.bibliographiccitation.volume","55"],["dc.contributor.author","Schaade, L."],["dc.contributor.author","Thomssen, R."],["dc.contributor.author","Ritter, K."],["dc.date.accessioned","2018-11-07T08:59:56Z"],["dc.date.available","2018-11-07T08:59:56Z"],["dc.date.issued","2000"],["dc.description.abstract","In the membrane of mouse macrophages two gangliosides were detected which inhibit the division of murine mastocytoma P815 turner cells. The two gangliosides were incorporated into the cytoplasmatic membrane of mastocytoma cells. The concentration necessary to achieve a complete inhibition of P815 tumor cell division is about 1 muM for both effective gangliosides. Macrophage ganglioside-induced inhibition of cell division is accompanied by morphological changes of the mastocytoma cells. While the cells art: rounding, their diameter increases and serotonin and granules appear in the cytoplasm of the enlarged cells. Our findings suggest that macrophage gangliosides may differentiate mastocytoma cells into mast cells."],["dc.identifier.isi","000166412500025"],["dc.identifier.pmid","11204177"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24021"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Walter De Gruyter Gmbh"],["dc.relation.issn","1865-7125"],["dc.relation.issn","0939-5075"],["dc.title","Differentiation in murine mastocytoma induced by macrophage gangliosides"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","408"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Medical Virology"],["dc.bibliographiccitation.lastpage","416"],["dc.bibliographiccitation.volume","71"],["dc.contributor.author","Dalpke, A. H."],["dc.contributor.author","Thomssen, R."],["dc.contributor.author","Ritter, K."],["dc.date.accessioned","2018-11-07T10:35:04Z"],["dc.date.available","2018-11-07T10:35:04Z"],["dc.date.issued","2003"],["dc.description.abstract","During the course of acute Epstein-Barr virus (EBV) infection, there is a rise of oxygen radical production. As a consequence, the production of the oxygen radical scavenger manganese superoxide dismutase (MnSOD) is increased. Patients with acute EBV infections regularly develop autoantibodies against MnSOD that are able to inhibit the enzyme activity in vitro. To elucidate the origin of the autoantibodies, the epitopes on MnSOD were determined. The entire sequence of MnSOD was synthesized as overlapping pentadecapeptides, which were scanned for their reactivity with sera of patients with acute EBV infections. Sera as well as affinity-purified anti-MnSOD antibodies reacted with the peptides p(no15) (amino acids 47-61) and p(no30) (amino acids 122-136) lying in crucial parts of the MnSOD tetramer. The two main epitopes p(no15) and p(no30) showed sequence homologies with EBV-encoded proteins. Reactivity of affinity-purified antibodies with a peptide of the homologous BGLF4 points to a molecular mimicry causing the occurrence of anti-MnSOD antibodies. Anti-MnSOD antibodies were able to block the protective effects of MnSOD in a model for oxidative damage produced by xanthine/xanthine oxidase in EAhy926 endothelial cells. Thus, these autoantibodies may contribute in vivo to the clinical symptoms by accumulation of toxic oxygen radicals."],["dc.identifier.doi","10.1002/jmv.10501"],["dc.identifier.isi","000185567600013"],["dc.identifier.pmid","12966547"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/45009"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-liss"],["dc.relation.issn","0146-6615"],["dc.title","Oxidative injury to endothelial cells due to Epstein-Barr virus-induced autoantibodies against manganese superoxide dismutase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","384"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","THERAPEUTIC APHERESIS"],["dc.bibliographiccitation.lastpage","386"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Schettler, Volker"],["dc.contributor.author","Monazahian, M."],["dc.contributor.author","Wieland, Eberhard"],["dc.contributor.author","Thomssen, R."],["dc.contributor.author","Mueller, Gerhard A."],["dc.date.accessioned","2018-11-07T08:38:03Z"],["dc.date.available","2018-11-07T08:38:03Z"],["dc.date.issued","2001"],["dc.description.abstract","Association of the hepatitis C virus (HCV) with apolipoprotein B containing lipoproteins has been suggested, and this led to the concept that the low-density lipoprotein (LDL) receptor may also serve as a candidate receptor for HCV uptake into the liver. We have investigated whether heparin-induced extracorporeal LDL precipitation (HELP) LDL apheresis treatment reduces HCV plasma load in 6 patients, all infected for more than 4 years with HCV and resistant against established anti-HCV therapy. HELP apheresis treatment caused an HCV-RNA decrease of 77.3% in mean. This decline was not correlated with LDL-cholesterol reduction. HCV-RNA was retained on the HELP filter as shown for 1 patient. The effect of RNA lowering was only transient due to the high turnover of HCV. However, HELP apheresis may open a window of opportunity for an immune-modulating and antiviral therapy in the interval between two apheresis procedures in patients with high virus load."],["dc.identifier.doi","10.1046/j.1526-0968.2001.00374.x"],["dc.identifier.isi","000174293700011"],["dc.identifier.pmid","11778924"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/18683"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Publishing Inc"],["dc.relation.issn","1091-6660"],["dc.title","Effect of heparin-induced extracorporeal low-density lipoprotein precipitation (HELP) apheresis on hepatitis C plasma virus load"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]