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  • 1
    Language: English
    In: Clinical and Molecular Allergy, April 1, 2010, Vol.8, p.7
    Description: Background Hymenoptera venoms are known to cause life-threatening IgE-mediated anaphylactic reactions in allergic individuals. Proper diagnosis of hymenoptera venom allergy using venom extracts is severely affected by molecular cross-reactivities. Although non-glycosylated marker allergens would facilitate the identification of the culprit venom, the major allergen phospholipase A1 (Ves v 1) from yellow jacket venom (YJV) remained unavailable so far. Methods Expression of Ves v 1 as wild type and enzymatically inactivated mutant and Ves v 5 in insect cells yielded soluble proteins that were purified via affinity chromatography. Functionality of the recombinant allergens was assessed by enzymatic and biophysical analyses as well as basophil activation tests. Diagnostic relevance was addressed by ELISA-based analyses of sera of YJV-sensitized patients. Results Both major allergens Ves v 1 and Ves v 5 could be produced in insect cells in secreted soluble form. The recombinant proteins exhibited their particular biochemical and functional characteristics and were capable for activation of human basophils. Assessment of IgE reactivity of sera of YJV-sensitized and double-sensitized patients emphasised the relevance of Ves v 1 in hymenoptera venom allergy. In contrast to the use of singular molecules the combined use of both molecules enabled a reliable assignment of sensitisation to YJV for more than 90% of double-sensitised patients. Conclusions The recombinant availability of Ves v 1 from yellow jacket venom will contribute to a more detailed understanding of the molecular and allergological mechanisms of insect venoms and may provide a valuable tool for diagnostic and therapeutic approaches in hymenoptera venom allergy.
    Keywords: Phospholipases -- Properties ; Yellow Jacket -- Health Aspects ; Wasp Venoms -- Properties ; Allergy -- Diagnosis ; Allergy -- Care And Treatment ; Allergy -- Genetic Aspects ; Hymenoptera -- Health Aspects ; Gene Expression -- Physiological Aspects ; Enzyme Kinetics -- Research
    ISSN: 1476-7961
    Source: Cengage Learning, Inc.
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  • 2
    Language: English
    In: The Journal of Allergy and Clinical Immunology, March 2014, Vol.133(3), pp.909-910
    Description: To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.jaci.2013.09.047 Byline: Liliana Cifuentes, Sebastian Vosseler, Simon Blank, Henning Seismann, Davide Pennino, Ulf Darsow, Reinhard Bredehorst, Johannes Ring, Martin Mempel, Edzard Spillner, Markus W. Ollert Author Affiliation: (a) Department of Dermatology and Allergy, Biederstein, Technical University Munich, Munich, Germany (b) Institute of Biochemistry and Molecular Biology, University of Hamburg, Hamburg, Germany (c) Center of Allergy and Environment (ZAUM), Technische Universitat and Helmholtz Center, Munich, Germany (d) Department of Dermatology, Venereology, and Allergology, Universitatsmedizin Gottingen, Gottingen, Germany Article Note: (footnote) This work was supported by the "Hochschulwissenschaftsprogramm" (HWP), "Kommission Klinische Forschung" (KKF) of the Technical University Munich, and the Christine Kuhne - Center for Allergy Research and Education (CK-CARE). L.C. and D.P. were supported by a scholarship of Bayerische Forschungsstiftung., Disclosure of potential conflict of interest: U. Darsow has consultant arrangements with Bencard and Leo and has received payment for lectures from Bencard and Novartis. R. Bredehorst is cofounder of PLS-Design Gmbh, which owns patent rights for Api m 3, Api m 5, and Ves v 3. J. Ring has received research support from ALK-Abello, Allergopharma, Almirall-Hermal, Astellas, Bencard, Biogen-Idec, Galderma, GlaxoSmithKline, Leo, Merck Sharp Dohme, Novartis, Phadia, PLS Design, and Stallergenes. E. Spillner is cofounder of PLS-Design GmbH. M. W. Ollert has consultant arrangements with Siemens Healthcare Diagnostics and Hitachi Chemical Diagnostics, has received payment for lectures from Phadia/Thermo Fisher, has received payment for education presentations from Siemens Healthcare Diagnostics, and is the scientific cofounder of the University of Hamburg biotech spin-off PLS-Design GmbH (Hamburg, Germany). The rest of the authors declare that they have no relevant conflicts of interest.
    Keywords: Medicine
    ISSN: 0091-6749
    E-ISSN: 1097-6825
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  • 3
    Language: English
    In: Analytical Biochemistry, 2011, Vol.412(2), pp.134-140
    Description: Anti-IgE therapeutics represent an efficient approach in the management of IgE-mediated allergic asthma. However, monitoring the reduction of IgE levels into a therapeutically efficient range requires the determination of residual serum IgE. We established an analytical approach to distinguish free and anti-IgE complexed serum IgE based on soluble derivatives of the human high-affinity IgE receptor. Soluble receptor derivatives represent an ideal means to analyze receptor antagonism by any ligand or blocking antibody. Therefore, the FcεRI ectodomain was fused with avian IgY constant domains that circumvent susceptibility to interference phenomena and improve assay performance. After production in HEK293 cells, subsequent characterization by enzyme-linked immunosorbent assay and immunoblotting confirmed the suitability of avian IgY constant domains for immobilization and detection purposes. To provide further insights into the different IgE reactivities, free allergen-specific IgE was also determined. Monitoring of sera from omalizumab-treated patients during the course of therapy revealed the applicability for assessment of omalizumab-complexed versus noncomplexed serum IgE. These parameters may allow correlation to clinical responses during anti-IgE therapy with the perspective of biomonitoring.
    Keywords: Ige ; Fcεri ; Anti-Ige ; Omalizumab ; Complex Formation ; Chemistry ; Anatomy & Physiology
    ISSN: 0003-2697
    E-ISSN: 1096-0309
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  • 4
    Language: English
    In: Analytical biochemistry, 2011, Vol.412(2), pp.134-140
    Description: Anti-IgE therapeutics represent an efficient approach in the management of IgE-mediated allergic asthma. However, monitoring the reduction of IgE levels into a therapeutically efficient range requires the determination of residual serum IgE. We established an analytical approach to distinguish free and anti-IgE complexed serum IgE based on soluble derivatives of the human high-affinity IgE receptor. Soluble receptor derivatives represent an ideal means to analyze receptor antagonism by any ligand or blocking antibody. Therefore, the FcεRI ectodomain was fused with avian IgY constant domains that circumvent susceptibility to interference phenomena and improve assay performance. After production in HEK293 cells, subsequent characterization by enzyme-linked immunosorbent assay and immunoblotting confirmed the suitability of avian IgY constant domains for immobilization and detection purposes. To provide further insights into the different IgE reactivities, free allergen-specific IgE was also determined. Monitoring of sera from omalizumab-treated patients during the course of therapy revealed the applicability for assessment of omalizumab-complexed versus noncomplexed serum IgE. These parameters may allow correlation to clinical responses during anti-IgE therapy with the perspective of biomonitoring. ; p. 134-140.
    Keywords: Blood Serum ; Therapeutics ; Monitoring ; Antibodies ; Immunoglobulin E ; Humans ; Immunoblotting ; Birds ; Chimerism ; Enzyme-Linked Immunosorbent Assay ; Patients ; Immunoglobulin Y ; Asthma
    ISSN: 0003-2697
    Source: AGRIS (Food and Agriculture Organization of the United Nations)
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  • 5
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 20 December 1994, Vol.91(26), pp.12775-12779
    Description: Cobra venom factor (CVF) is the complement-activating protein in cobra venom. Like C3b, CVF forms with factor B and factor D in human and mammalian serum the bimolecular C3/C5 convertase. This functional similarity of CVF and C3 correlates with many structural similarities, which led to the suggestion that CVF is evolutionally related to C3. We report here the molecular cloning and derived primary structure of CVF. CVF mRNA is 〉5924 nucleotides in length. It contains a single open reading frame of 4926 nucleotides, coding for a pre-pro-protein of 1642 amino acids. The deduced amino acid sequence reveals ≈70% protein similarity to mammalian and human C3 and exceeds 91% in the case of cobra C3. The single-chain pre-pro-CVF consists of a 22-amino acid signal sequence, a 627-amino acid α-chain, and a 989-amino acid precursor chain for the CVF γ- and β-chains. The processing of pro-CVF involves the removal of 4 arginine residues between the α- and precursor chains as well as of the C3a-like and C3d-like domains from the precursor chain, thereby confirming the predicted chain homologies to C3. Pro-CVF contains five potential N-glycosylation sites, of which only three can be expected to be glycosylated in mature CVF. Like C3, pro-CVF contains 27 cysteine residues and a homologous thioester site in the C3d-like region.
    Keywords: Physical sciences -- Physics -- Microphysics ; Physical sciences -- Chemistry -- Chemical compounds ; Physical sciences -- Chemistry -- Chemical compounds ; Biological sciences -- Biology -- Physiology ; Physical sciences -- Chemistry -- Chemical compounds ; Biological sciences -- Biochemistry -- Enzymology ; Physical sciences -- Physics -- Microphysics ; Biological sciences -- Biology -- Genetics ; Behavioral sciences -- Anthropology -- Applied anthropology ; Biological sciences -- Biology -- Genetics
    ISSN: 00278424
    E-ISSN: 10916490
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  • 6
    Language: English
    In: Clinical and Molecular Allergy, April 1, 2010, Vol.8, p.7
    Description: Background Hymenoptera venoms are known to cause life-threatening IgE-mediated anaphylactic reactions in allergic individuals. Proper diagnosis of hymenoptera venom allergy using venom extracts is severely affected by molecular cross-reactivities. Although non-glycosylated marker allergens would facilitate the identification of the culprit venom, the major allergen phospholipase A1 (Ves v 1) from yellow jacket venom (YJV) remained unavailable so far. Methods Expression of Ves v 1 as wild type and enzymatically inactivated mutant and Ves v 5 in insect cells yielded soluble proteins that were purified via affinity chromatography. Functionality of the recombinant allergens was assessed by enzymatic and biophysical analyses as well as basophil activation tests. Diagnostic relevance was addressed by ELISA-based analyses of sera of YJV-sensitized patients. Results Both major allergens Ves v 1 and Ves v 5 could be produced in insect cells in secreted soluble form. The recombinant proteins exhibited their particular biochemical and functional characteristics and were capable for activation of human basophils. Assessment of IgE reactivity of sera of YJV-sensitized and double-sensitized patients emphasised the relevance of Ves v 1 in hymenoptera venom allergy. In contrast to the use of singular molecules the combined use of both molecules enabled a reliable assignment of sensitisation to YJV for more than 90% of double-sensitised patients. Conclusions The recombinant availability of Ves v 1 from yellow jacket venom will contribute to a more detailed understanding of the molecular and allergological mechanisms of insect venoms and may provide a valuable tool for diagnostic and therapeutic approaches in hymenoptera venom allergy.
    Keywords: Phospholipases -- Properties ; Yellow Jacket -- Health Aspects ; Wasp Venoms -- Properties ; Allergy -- Diagnosis ; Allergy -- Care And Treatment ; Allergy -- Genetic Aspects ; Hymenoptera -- Health Aspects ; Gene Expression -- Physiological Aspects ; Enzyme Kinetics -- Research
    ISSN: 1476-7961
    Source: Cengage Learning, Inc.
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  • 7
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 01 August 1995, Vol.92(16), pp.7605-7605
    Keywords: Biological sciences -- Biochemistry -- Biomolecules
    ISSN: 00278424
    E-ISSN: 10916490
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  • 8
    Language: English
    In: Clinical and Molecular Allergy, 01 April 2010, Vol.8(1), p.7
    Description: Abstract Background Hymenoptera venoms are known to cause life-threatening IgE-mediated anaphylactic reactions in allergic individuals. Proper diagnosis of hymenoptera venom allergy using venom extracts is severely affected by molecular cross-reactivities. Although non-glycosylated marker allergens would facilitate the identification of the culprit venom, the major allergen phospholipase A1 (Ves v 1) from yellow jacket venom (YJV) remained unavailable so far. Methods Expression of Ves v 1 as wild type and enzymatically inactivated mutant and Ves v 5 in insect cells yielded soluble proteins that were purified via affinity chromatography. Functionality of the recombinant allergens was assessed by enzymatic and biophysical analyses as well as basophil activation tests. Diagnostic relevance was addressed by ELISA-based analyses of sera of YJV-sensitized patients. Results Both major allergens Ves v 1 and Ves v 5 could be produced in insect cells in secreted soluble form. The recombinant proteins exhibited their particular biochemical and functional characteristics and were capable for activation of human basophils. Assessment of IgE reactivity of sera of YJV-sensitized and double-sensitized patients emphasised the relevance of Ves v 1 in hymenoptera venom allergy. In contrast to the use of singular molecules the combined use of both molecules enabled a reliable assignment of sensitisation to YJV for more than 90% of double-sensitised patients. Conclusions The recombinant availability of Ves v 1 from yellow jacket venom will contribute to a more detailed understanding of the molecular and allergological mechanisms of insect venoms and may provide a valuable tool for diagnostic and therapeutic approaches in hymenoptera venom allergy.
    Keywords: Medicine
    ISSN: 1476-7961
    E-ISSN: 1476-7961
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  • 9
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 01 December 1986, Vol.83(23), pp.9144-9148
    Description: Human melanoma cells resistant to killing by monoclonal antibody R24 plus human complement became susceptible after treatment with doxorubicin (adriamycin). Treatment with doxorubicin prevented the rapid degradation of surface-bound complement component C3b that has been identified as a protective mechanism of complement-resistant melanoma cells. Doxorubicin caused the increased complement susceptibility as free drug and after immobilization onto glass beads to prevent cellular uptake. Immobilized doxorubicin was more effective than free drug, causing enhanced complement susceptibility at concentrations where the free drug was no longer active. In contrast to free doxorubicin, which exhibited a direct cytotoxic effect leading to cell death within 4 days, immobilized doxorubicin did not affect cell viability. These findings suggest that combination therapy of the complement-activating monoclonal antibody R24 with the complement-enhancing drug doxorubicin may be a promising approach for the treatment of melanoma.
    Keywords: Biological sciences -- Biology -- Cytology -- Monoclonal antibodies ; Health sciences -- Medical conditions -- Diseases -- Monoclonal antibodies ; Health sciences -- Medical sciences -- Immunology -- Monoclonal antibodies ; Health sciences -- Health and wellness -- Public health -- Monoclonal antibodies ; Health sciences -- Medical sciences -- Immunology -- Monoclonal antibodies ; Behavioral sciences -- Psychology -- Cognitive psychology -- Monoclonal antibodies ; Biological sciences -- Biology -- Cytology -- Monoclonal antibodies ; Health sciences -- Medical sciences -- Immunology -- Monoclonal antibodies ; Health sciences -- Medical sciences -- Immunology -- Monoclonal antibodies ; Applied sciences -- Materials science -- Materials processing -- Monoclonal antibodies
    ISSN: 00278424
    E-ISSN: 10916490
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  • 10
    In: Analytical Chemistry, Jan 15, 1997, Vol.69(2), p.175(8)
    Description: The intrinsic binding characteristics of monoclonal antibodies are modified upon immobilization onto a solid-phase matrix. Factors such as the distribution in affinity must therefore be taken into consideration in order to predict the kinetics of antibody binding at solid-liquid interfaces. A mathematical analysis is presented herein that allows the assessment of heterogeneity in the affinity of monoclonal antibodies immobilized onto a solid support. This model is based on a modified version of the Sips distribution function adapted to the conditions of a solid-phase displacement assay in flow. An assay for trinitrotoluene (TNT) provides the data to evaluate the extent of heterogeneity introduced by immobilization of antibodies in a flow immunoassay. We determined the index of antibody heterogeneity on two solid supports, controlled-pore glass beads and agarose beads, coated with a monoclonal anti-TNT antibody at varying densities. The data confirm that the threshold for crossover from homogeneous to heterogeneous forms of the reaction isotherm is different in displacement reactions than in association - dissociation reactions. Our analysis shows that the measured displacement isotherm is consistent with a homogeneous or only moderately heterogenous distribution of relative affinities.
    Keywords: Antigen-antibody Reactions -- Analysis ; Monoclonal Antibodies -- Analysis
    ISSN: 0003-2700
    E-ISSN: 15206882
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