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  • 1
    Keywords: PEPTIDE ; RECEPTOR ; CELLS ; tumor ; TUMOR-CELLS ; BLOOD ; CELL ; Germany ; THERAPY ; POPULATION ; PROTEIN ; LINES ; PATIENT ; DNA ; IFN-GAMMA ; MOTIFS ; DONOR ; ANTIGEN ; DENDRITIC CELLS ; SKIN ; T cells ; T-CELLS ; IDENTIFICATION ; LYMPHOMA ; ASSAY ; LINE ; BETA ; PEPTIDES ; EPITOPE ; EPITOPES ; IMMUNOTHERAPY ; TCR ; TARGETS ; FUTURE ; PERIPHERAL-BLOOD ; TUMOR CELLS ; MONONUCLEAR-CELLS ; TUMOR-ASSOCIATED ANTIGENS ; RE ; cutaneous T-cell lymphoma ; TUMOR-CELL ; UNIT ; PLASMID ; peripheral blood ; peripheral blood mononuclear cells ; LYMPHOPROLIFERATIONS ; MELANOMA ANTIGEN ; reverse immunology
    Abstract: The clonotypic T-cell receptor (TCR) is a potential target antigen for specific immunotherapy of cutaneous T-cell lymphoma (CTCL). We identified T-cell epitopes from the rearranged TCR beta chain of the malignant T-cell population by the "reverse immunology" approach. Peptide-specific T-cell lines were generated against predicted epitopes and tested for the recognition of tumor cells and cells transfected with the full-length DNA coding for TCRV beta chain. Two peptides derived from the clonotypic TCRV beta of a HLA-A2 positive patient could induce peptide-specific T cells from peripheral blood mononuclear cells of healthy donors and the patient as assessed by IFN-gamma ELISpot assay. Furthermore, the reactive CTLs efficiently recognized autologous Sezary tumor cells, as well as HLA-A2 positive 293 cells transfected with recombinant plasmid expressing the corresponding TCRV beta 29 protein. Similar results were obtained in a HLA-A3+ patient for TCRV beta 7-J beta 2.7. In conclusion, our experiments show that the TCR beta chain harbors epitopes suitable as targets for specific vaccination which might be a promising approach for the specific immunotherapy of cutaneous T-cell lymphoma patients. (c) 2006 Wiley-Liss, Inc
    Type of Publication: Journal article published
    PubMed ID: 16858680
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  • 2
    Keywords: RECEPTOR ; APOPTOSIS ; CELLS ; IN-VITRO ; CELL ; Germany ; human ; VITRO ; SYSTEM ; SYSTEMS ; DISEASE ; GENE ; GENE-EXPRESSION ; PROTEIN ; RNA ; transcription ; MOLECULES ; RESPONSES ; DNA ; kidney ; MECHANISM ; INDUCTION ; CONTRAST ; mechanisms ; SIGNAL ; MOLECULE ; IMMUNE-RESPONSES ; STIMULATION ; virus ; VECTOR ; SURFACE ; immune response ; IMMUNE-RESPONSE ; ADAPTIVE IMMUNITY ; CELL-SURFACE ; DANGER ; danger signal ; DOUBLE-STRANDED-RNA ; GREECE ; HN ; I INTERFERON ; INTERFERON-ALPHA ; NDV ; NEWCASTLE-DISEASE VIRUS ; poly(I : C) ; RECEPTORS ; SFV
    Abstract: In order to study mechanisms of induction of IFN-alpha by Newcastle disease virus (NDV), we used two replicon systems which are based respectively on DNA and RNA of the Semliki forest virus (SFV) and transfected these into baby hamster kidney cells (BHK) which do not produce interferon-alpha. Co-incubation of BHK cells which were transfected with the two vector systems, with human PBMCs, showed that production of IFN-alpha takes place by two different ways. When using the DNA-based SFV vector, only transfectants expressing cell surface HN molecules of NDV (and not the mock-transfected cells) elicited such a response via interaction of these HN molecules with viral receptors on PBMCs. In contrast, BHK cells transfected with RNA which had been in vitro transcribed from the RNA-based SFV vector without foreign gene as insert (mock-transfected) elicited a comparable IFN-alpha response. Transfer by transfection of poly(I:C), an analogue of double stranded RNA (dsRNA), into the BHK cells induced also by itself the production of IFN-alpha. Therefore induction of 'danger signals' (as double-strand RNA replicative intermediates) might be responsible for this discrepancy observed in IFN-alpha induction in PBMCs between the two studied SFV vector systems based on transfection of DNA and on RNA. These observations highlight two ways of IFN-alpha induction which additively may explain the high interferonogenic capacity of NDV as virus: i) via cell-surface expressed HN after transfection of the DNA-based SFV replicon and ii) via transfection of self-amplifying RNA
    Type of Publication: Journal article published
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  • 3
    Keywords: CELLS ; EXPRESSION ; IN-VITRO ; CELL ; Germany ; VITRO ; SYSTEM ; DISEASE ; GENE ; PROTEIN ; PROTEINS ; RNA ; cell line ; MOLECULES ; LINES ; TIME ; DNA ; CELL-LINES ; MOLECULE ; CLEAVAGE ; virus ; VECTORS ; PROMOTER ; CELL-LINE ; FUSION ; LINE ; MUTATIONS ; SURFACE ; VACCINE ; CLEAVAGE SITE ; GREECE ; HN ; NDV ; protein expression ; HIGH-LEVEL ; F ; ENHANCER ; CRYSTALLIZATION ; HEMAGGLUTININ-NEURAMINIDASE PROTEIN ; PARAMYXOVIRUS FUSION ; Semliki Forest virus ; SEMLIKI-FOREST-VIRUS ; syncytium ; VIRAL MEMBRANE-FUSION ; VIRULENCE
    Abstract: For functional studies, the hemagglutinin-neuraminidase (HN) and the fusion protein (F) of Newcastle disease virus (NDV) were expressed in BHK cells using two vectors which are based on the Semliki Forest virus (SFV) replicon. The first system of high protein expression works by transfection of RNA which before has been in vitro transcribed from a vector containing the gene for the SFV self-amplifying replicase (REP) and a foreign gene using the SP6 promoter. A high level of protein (HN or F) expression was detected 18-20 h after transfection. To study the host range of this expression system, a panel of different cell lines were compared for transfections with SFV RNA. A wide range of expression efficiency was observed, the highest being BHK cells. The second system is based on a DNA plasmid in which the SFV-REP and a foreign gene are expressed in cells under the transcriptional and translational control of the cytomegalovirus immediate-early enhancer T7 promoter. DNA-electroporated BHK cells expressed also high levels of the recombinant proteins but at a delayed time point (40-48 h) as compared with the corresponding RNA. Co-expression of the two NDV proteins, HN and F, via this DNA vector in the same cells led to syncytium formation in the cell monolayer, showing that both proteins expressed in this way, were functionally active. F alone, expressed via this vector, displayed residual fusion activity suggesting its proteolytic cleavage and its functional independence from HN
    Type of Publication: Journal article published
    PubMed ID: 15254725
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  • 4
    Keywords: CELLS ; EXPRESSION ; tumor ; TUMOR-CELLS ; CELL ; Germany ; human ; DISEASE ; SITE ; CLONING ; DISTINCT ; GENE ; GENES ; PROTEIN ; MOLECULES ; LIGAND ; T cell ; T-CELL ; SEQUENCE ; MOLECULE ; ACID ; antibodies ; antibody ; GLYCOPROTEIN ; virus ; ASSAY ; DIFFERENCE ; FUSION ; MELANOMA ; SURFACE ; GREECE ; INTERFERON-ALPHA ; SEQUENCE-ANALYSIS ; M1 ; ENDOPLASMIC-RETICULUM ; F-PROTEIN ; HN PROTEIN ; INFLUENZA-VIRUS ; NDV,mutant,hemagglutinin,structure,molecular modeling,tumor vaccine,virotherapy ; PARAMYXOVIRIDAE ATTACHMENT PROTEINS ; RECEPTOR RECOGNITION ; STRUCTURE ALIGNMENT
    Abstract: Newcastle Disease Virus (NDV) is an avian paramyxovirus with replication competence in human tumor cells and interesting anti-neoplastic and immune stimulatory properties. In order to increase tumor selectivity of replication, we prepared mutants from the avirulent strain Ulster with monocyclic replication cycle and adapted them for multi-cyclic replication in human melanoma cells. Two mutants (M1 and M2) showed interesting functional differences: while M2 showed T cell co-stimulatory effects in a tumor-specific cytotoxic T lymphocyte (CTL) assay, M1 did not. A distinct difference of these 2 virus mutants appeared also when testing their capacity to induce interferon-alpha and -beta as well as tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) molecules in human monocytes. Sequence analysis of the hemagglutinin-neuraminidase (HN) molecules of the 2 virus mutants showed 7 non-silent mutational differences. Upon cloning of the HN mutant genes into an expression vector and transfection of cells, only HN derived from M2 (HN-M2) was detected at the cell surface by immunostaining with specific antibodies and showed hemadsorption and neuraminidase activity. In order to define which amino acid was responsible for the loss of functional activity of HN derived from M1 (HN-M1), distinct HN mutants were generated via site-directed mutagenesis and tested. Substitution of serine 200 by a proline abrogated HN expression and its hemadsorption and neuraminidase activities. Molecular modeling revealed that proline 200 in HN influences flexibility of a loop near the entrance to the neuraminidase active site, a function that may be crucial for the functions of this viral protein
    Type of Publication: Journal article published
    PubMed ID: 14767547
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  • 5
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Nuclear Physics, Section A 414 (1984), S. 253-268 
    ISSN: 0375-9474
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Nuclear Physics, Section A 411 (1983), S. 49-64 
    ISSN: 0375-9474
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Nuclear Physics, Section A 421 (1984), S. 125-139 
    ISSN: 0375-9474
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Nuclear Physics, Section A 405 (1983), S. 1-28 
    ISSN: 0375-9474
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
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