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  1. Article: [No title information]

    Wenzel, Esther Veronika / Zilkens, Kilian Johannes Carl

    Biospektrum : Zeitschrift der Gesellschaft fur Biologishe Chemie (GBCH) und der Vereinigung fur Allgemeine und Angewandte Mikrobiologie (VAAM)

    2022  Volume 28, Issue 2, Page(s) 178–179

    Abstract: Despite readily available alternative technologies, many antibodies in research and diagnostics are still generated and produced with the use of laboratory animals. Here, we portrait the concept of animal-free recombinant antibodies and the generation of ...

    Title translation Rekombinante Antikörper als Alternativen in Forschung und Diagnostik.
    Abstract Despite readily available alternative technologies, many antibodies in research and diagnostics are still generated and produced with the use of laboratory animals. Here, we portrait the concept of animal-free recombinant antibodies and the generation of such an antibody against the spike-protein of SARS-Cov-2. The scientific community needs to raise awareness for more sustainable animal-free alternatives, especially as they offer a path to more reliable and reproducible data.
    Language German
    Publishing date 2022-03-28
    Publishing country Germany
    Document type English Abstract ; Journal Article
    ZDB-ID 2203536-9
    ISSN 1868-6249 ; 0947-0867
    ISSN (online) 1868-6249
    ISSN 0947-0867
    DOI 10.1007/s12268-022-1716-7
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  2. Article: [No title information]

    Wenzel, Esther Veronika / Russo, Giulio / Dübel, Stefan

    Biospektrum : Zeitschrift der Gesellschaft fur Biologishe Chemie (GBCH) und der Vereinigung fur Allgemeine und Angewandte Mikrobiologie (VAAM)

    2020  Volume 26, Issue 4, Page(s) 416–417

    Abstract: Today, recombinant antibodies can replace animal-derived primary antibodies in almost all applications. Due to their monoclonal origin and always known sequence, they offer optimal reproducibility. In contrast, almost all secondary antibodies are still ... ...

    Title translation Multiklonale Antikörper als Ersatz für Zweitantikörper aus Seren.
    Abstract Today, recombinant antibodies can replace animal-derived primary antibodies in almost all applications. Due to their monoclonal origin and always known sequence, they offer optimal reproducibility. In contrast, almost all secondary antibodies are still made from animal sera. Multiclonal antibodies made by animal-free recombinant methods here offer a higher quality replacement for serum-derived secondary antibodies.
    Keywords covid19
    Language German
    Publishing date 2020-06-26
    Publishing country Germany
    Document type English Abstract ; Journal Article
    ZDB-ID 2203536-9
    ISSN 1868-6249 ; 0947-0867
    ISSN (online) 1868-6249
    ISSN 0947-0867
    DOI 10.1007/s12268-020-1401-7
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  3. Article ; Online: Antibody Selection in Solution Using Magnetic Beads.

    Heine, Philip Alexander / Ruschig, Maximilian / Langreder, Nora / Wenzel, Esther Veronika / Schubert, Maren / Bertoglio, Federico / Hust, Michael

    Methods in molecular biology (Clifton, N.J.)

    2023  Volume 2702, Page(s) 261–274

    Abstract: Antibody phage display is a valuable in vitro technology to generate recombinant, sequence-defined antibodies for research, diagnostics, and therapy. Up to now (autumn 2022), 14 FDA/EMA-approved therapeutic antibodies were developed using phage display, ... ...

    Abstract Antibody phage display is a valuable in vitro technology to generate recombinant, sequence-defined antibodies for research, diagnostics, and therapy. Up to now (autumn 2022), 14 FDA/EMA-approved therapeutic antibodies were developed using phage display, including the world best-selling antibody adalimumab. Additionally, recombinant, sequence-defined antibodies have significant advantages over their polyclonal counterparts.For a successful in vitro antibody generation by phage display, a suitable panning strategy is highly important. We present in this book chapter the panning in solution and its advantages over panning with immobilized antigens and give detailed protocols for the panning and screening procedure.
    MeSH term(s) Antibodies ; Cell Surface Display Techniques ; Seasons ; Technology ; Magnetic Phenomena
    Chemical Substances Antibodies
    Language English
    Publishing date 2023-08-23
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-3381-6_13
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  4. Article: Investigating Alternative Container Formats for Lyophilization of Biological Materials Using Diphtheria Antitoxin Monoclonal Antibody as a Model Molecule.

    Malik, Kiran P / Duru, Chinwe / Stickings, Paul / Wenzel, Esther Veronika / Hust, Michael / Matejtschuk, Paul

    Pharmaceutics

    2021  Volume 13, Issue 11

    Abstract: When preparing biological reference materials, the stability of the lyophilized product is critical for long-term storage, particularly in order to meet WHO International Standards, which are not assigned expiry dates but are expected to be in use for ... ...

    Abstract When preparing biological reference materials, the stability of the lyophilized product is critical for long-term storage, particularly in order to meet WHO International Standards, which are not assigned expiry dates but are expected to be in use for several decades. Glass ampoules are typically used by the National Institute for Biological Standards and Control (NIBSC) for the lyophilization of biological materials. More recently, a clear need has arisen for the filling of smaller volumes, for which ampoules may not be optimal. We investigated the use of plastic microtubes as an alternative container for small volume fills. In this study, a recombinant diphtheria antitoxin monoclonal antibody (DATMAB) was used as a model molecule to investigate the suitability of plastic microtubes for filling small volumes. The stability and quality of the dried material was assessed after an accelerated degradation study using a toxin neutralization test and size exclusion HPLC. While microtubes have shown some promise in the past for use in the lyophilization of some biological materials, issues with stability may arise when more labile materials are freeze-dried. We demonstrate here that the microtube format is unsuitable for ensuring the stability of this monoclonal antibody.
    Language English
    Publishing date 2021-11-17
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2527217-2
    ISSN 1999-4923
    ISSN 1999-4923
    DOI 10.3390/pharmaceutics13111948
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Book ; Online ; Thesis: Development of recombinant human anti-diphtheria toxin neutralizing antibodies for diphtheria therapy

    Wenzel, Esther Veronika [Verfasser] / Hust, Michael [Akademischer Betreuer] / Dübel, Stefan [Akademischer Betreuer]

    2019  

    Author's details Esther Veronika Wenzel ; Michael Hust, Stefan Dübel
    Keywords Medizin, Gesundheit ; Medicine, Health
    Subject code sg610
    Language English
    Publisher Technische Universität Braunschweig
    Publishing place Braunschweig
    Document type Book ; Online ; Thesis
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  6. Article ; Online: In vitro

    Russo, Giulio / Unkauf, Tobias / Meier, Doris / Wenzel, Esther Veronika / Langreder, Nora / Schneider, Kai-Thomas / Wiesner, Rebecca / Bischoff, Ralf / Stadler, Volker / Dübel, Stefan

    Biological chemistry

    2022  Volume 403, Issue 5-6, Page(s) 479–494

    Abstract: One of the most widely used epitope tags is the myc-tag, recognized by the anti-c-Myc hybridoma antibody Myc1-9E10. Combining error-prone PCR, DNA shuffling and phage display, we generated an anti-c-Myc antibody variant (Hyper-Myc) with monovalent ... ...

    Abstract One of the most widely used epitope tags is the myc-tag, recognized by the anti-c-Myc hybridoma antibody Myc1-9E10. Combining error-prone PCR, DNA shuffling and phage display, we generated an anti-c-Myc antibody variant (Hyper-Myc) with monovalent affinity improved to 18 nM and thermal stability increased by 37%. Quantification of capillary immunoblots and by flow cytometry demonstrated improved antigen detection by Hyper-Myc. Further, three different species variants of this antibody were generated to allow the use of either anti-human, anti-mouse or anti-rabbit Fc secondary antibodies for detection. We characterized the specificity of both antibodies in depth: individual amino acid exchange mapping demonstrated that the recognized epitope was not changed by the
    MeSH term(s) Animals ; Antibodies, Monoclonal/chemistry ; Epitope Mapping ; Epitopes ; Mice ; Proto-Oncogene Proteins c-myc/genetics ; Rabbits ; Zebrafish
    Chemical Substances Antibodies, Monoclonal ; Epitopes ; Proto-Oncogene Proteins c-myc
    Language English
    Publishing date 2022-03-22
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1334659-3
    ISSN 1437-4315 ; 1431-6730 ; 1432-0355
    ISSN (online) 1437-4315
    ISSN 1431-6730 ; 1432-0355
    DOI 10.1515/hsz-2021-0405
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
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  7. Article ; Online: Shelf-Life Extension of Fc-Fused Single Chain Fragment Variable Antibodies by Lyophilization.

    Schneider, Kai-Thomas / Kirmann, Toni / Wenzel, Esther Veronika / Grosch, Jan-Hendrik / Polten, Saskia / Meier, Doris / Becker, Marlies / Matejtschuk, Paul / Hust, Michael / Russo, Giulio / Dübel, Stefan

    Frontiers in cellular and infection microbiology

    2021  Volume 11, Page(s) 717689

    Abstract: Generation of sequence defined antibodies from universal libraries by phage display has been established over the past three decades as a robust method to cope with the increasing market demand in therapy, diagnostics and research. For applications ... ...

    Abstract Generation of sequence defined antibodies from universal libraries by phage display has been established over the past three decades as a robust method to cope with the increasing market demand in therapy, diagnostics and research. For applications requiring the bivalent antigen binding and an Fc part for detection, phage display generated single chain Fv (scFv) antibody fragments can rapidly be genetically fused to the Fc moiety of an IgG for the production in eukaryotic cells of antibodies with IgG-like properties. In contrast to conversion of scFv into IgG format, the conversion to scFv-Fc requires only a single cloning step, and provides significantly higher yields in transient cell culture production than IgG. ScFv-Fcs can be effective as neutralizing antibodies
    MeSH term(s) Antibodies, Neutralizing ; Cell Surface Display Techniques ; Freeze Drying ; Life Expectancy ; Single-Chain Antibodies/genetics
    Chemical Substances Antibodies, Neutralizing ; Single-Chain Antibodies
    Language English
    Publishing date 2021-11-15
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2619676-1
    ISSN 2235-2988 ; 2235-2988
    ISSN (online) 2235-2988
    ISSN 2235-2988
    DOI 10.3389/fcimb.2021.717689
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  8. Article ; Online: Baculovirus-Free SARS-CoV-2 Virus-like Particle Production in Insect Cells for Rapid Neutralization Assessment.

    Jaron, Marcel / Lehky, Michael / Zarà, Marta / Zaydowicz, Chris Nicole / Lak, Aidin / Ballmann, Rico / Heine, Philip Alexander / Wenzel, Esther Veronika / Schneider, Kai-Thomas / Bertoglio, Federico / Kempter, Susanne / Köster, Reinhard Wolfgang / Barbieri, Silvia Stella / van den Heuvel, Joop / Hust, Michael / Dübel, Stefan / Schubert, Maren

    Viruses

    2022  Volume 14, Issue 10

    Abstract: Virus-like particles (VLPs) resemble authentic virus while not containing any genomic information. Here, we present a fast and powerful method for the production of SARS-CoV-2 VLP in insect cells and the application of these VLPs to evaluate the ... ...

    Abstract Virus-like particles (VLPs) resemble authentic virus while not containing any genomic information. Here, we present a fast and powerful method for the production of SARS-CoV-2 VLP in insect cells and the application of these VLPs to evaluate the inhibition capacity of monoclonal antibodies and sera of vaccinated donors. Our method avoids the baculovirus-based approaches commonly used in insect cells by employing direct plasmid transfection to co-express SARS-CoV-2 envelope, membrane, and spike protein that self-assemble into VLPs. After optimization of the expression plasmids and vector ratios, VLPs with an ~145 nm diameter and the typical "Corona" aura were obtained, as confirmed by nanoparticle tracking analysis (NTA) and transmission electron microscopy (TEM). Fusion of the membrane protein to GFP allowed direct quantification of binding inhibition to angiotensin II-converting enzyme 2 (ACE2) on cells by therapeutic antibody candidates or sera from vaccinated individuals. Neither VLP purification nor fluorescent labeling by secondary antibodies are required to perform these flow cytometric assays.
    MeSH term(s) Humans ; Animals ; Baculoviridae/genetics ; SARS-CoV-2/genetics ; Angiotensin-Converting Enzyme 2 ; Spike Glycoprotein, Coronavirus/genetics ; Angiotensin II ; COVID-19 ; Insecta ; Antibodies, Monoclonal
    Chemical Substances Angiotensin-Converting Enzyme 2 (EC 3.4.17.23) ; Spike Glycoprotein, Coronavirus ; Angiotensin II (11128-99-7) ; Antibodies, Monoclonal
    Language English
    Publishing date 2022-09-20
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v14102087
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  9. Article ; Online: Developing Recombinant Antibodies by Phage Display Against Infectious Diseases and Toxins for Diagnostics and Therapy.

    Roth, Kristian Daniel Ralph / Wenzel, Esther Veronika / Ruschig, Maximilian / Steinke, Stephan / Langreder, Nora / Heine, Philip Alexander / Schneider, Kai-Thomas / Ballmann, Rico / Fühner, Viola / Kuhn, Philipp / Schirrmann, Thomas / Frenzel, André / Dübel, Stefan / Schubert, Maren / Moreira, Gustavo Marçal Schmidt Garcia / Bertoglio, Federico / Russo, Giulio / Hust, Michael

    Frontiers in cellular and infection microbiology

    2021  Volume 11, Page(s) 697876

    Abstract: Antibodies are essential molecules for diagnosis and treatment of diseases caused by pathogens and their toxins. Antibodies were integrated in our medical repertoire against infectious diseases more than hundred years ago by using animal sera to treat ... ...

    Abstract Antibodies are essential molecules for diagnosis and treatment of diseases caused by pathogens and their toxins. Antibodies were integrated in our medical repertoire against infectious diseases more than hundred years ago by using animal sera to treat tetanus and diphtheria. In these days, most developed therapeutic antibodies target cancer or autoimmune diseases. The COVID-19 pandemic was a reminder about the importance of antibodies for therapy against infectious diseases. While monoclonal antibodies could be generated by hybridoma technology since the 70ies of the former century, nowadays antibody phage display, among other display technologies, is robustly established to discover new human monoclonal antibodies. Phage display is an
    MeSH term(s) Animals ; Antibodies, Monoclonal ; Bacteriophages ; COVID-19 ; Communicable Diseases/diagnosis ; Communicable Diseases/therapy ; Humans ; Pandemics ; SARS-CoV-2
    Chemical Substances Antibodies, Monoclonal
    Language English
    Publishing date 2021-07-07
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2619676-1
    ISSN 2235-2988 ; 2235-2988
    ISSN (online) 2235-2988
    ISSN 2235-2988
    DOI 10.3389/fcimb.2021.697876
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  10. Article ; Online: Human antibodies neutralizing diphtheria toxin in vitro and in vivo.

    Wenzel, Esther Veronika / Bosnak, Margarita / Tierney, Robert / Schubert, Maren / Brown, Jeffrey / Dübel, Stefan / Efstratiou, Androulla / Sesardic, Dorothea / Stickings, Paul / Hust, Michael

    Scientific reports

    2020  Volume 10, Issue 1, Page(s) 571

    Abstract: Diphtheria is an infectious disease caused by Corynebacterium diphtheriae. The bacterium primarily infects the throat and upper airways and the produced diphtheria toxin (DT), which binds to the elongation factor 2 and blocks protein synthesis, can ... ...

    Abstract Diphtheria is an infectious disease caused by Corynebacterium diphtheriae. The bacterium primarily infects the throat and upper airways and the produced diphtheria toxin (DT), which binds to the elongation factor 2 and blocks protein synthesis, can spread through the bloodstream and affect organs, such as the heart and kidneys. For more than 125 years, the therapy against diphtheria has been based on polyclonal horse sera directed against DT (diphtheria antitoxin; DAT). Animal sera have many disadvantages including serum sickness, batch-to-batch variation in quality and the use of animals for production. In this work, 400 human recombinant antibodies were generated against DT from two different phage display panning strategies using a human immune library. A panning in microtiter plates resulted in 22 unique in vitro neutralizing antibodies and a panning in solution combined with a functional neutralization screening resulted in 268 in vitro neutralizing antibodies. 61 unique antibodies were further characterized as scFv-Fc with 35 produced as fully human IgG1. The best in vitro neutralizing antibody showed an estimated relative potency of 454 IU/mg and minimal effective dose 50% (MED50%) of 3.0 pM at a constant amount of DT (4x minimal cytopathic dose) in the IgG format. The targeted domains of the 35 antibodies were analyzed by immunoblot and by epitope mapping using phage display. All three DT domains (enzymatic domain, translocation domain and receptor binding domain) are targets for neutralizing antibodies. When toxin neutralization assays were performed at higher toxin dose levels, the neutralizing capacity of individual antibodies was markedly reduced but this was largely compensated for by using two or more antibodies in combination, resulting in a potency of 79.4 IU/mg in the in vivo intradermal challenge assay. These recombinant antibody combinations are candidates for further clinical and regulatory development to replace equine DAT.
    MeSH term(s) Animals ; Antibodies, Neutralizing/administration & dosage ; Antibodies, Neutralizing/pharmacology ; Corynebacterium diphtheriae/immunology ; Corynebacterium diphtheriae/metabolism ; Diphtheria Toxin/antagonists & inhibitors ; Diphtheria Toxin/chemistry ; Epitope Mapping/methods ; Guinea Pigs ; Humans ; Immunoglobulin G/pharmacology ; Injections, Intradermal ; Models, Molecular ; Peptide Elongation Factor 2/metabolism ; Peptide Library ; Protein Conformation ; Single-Chain Antibodies/pharmacology
    Chemical Substances Antibodies, Neutralizing ; Diphtheria Toxin ; Immunoglobulin G ; Peptide Elongation Factor 2 ; Peptide Library ; Single-Chain Antibodies
    Keywords covid19
    Language English
    Publishing date 2020-01-17
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-019-57103-5
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