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  1. Article ; Online: Animal- versus

    Bradbury, Andrew R M / Dübel, Stefan / Knappik, Achim / Plückthun, Andreas

    mAbs

    2021  Volume 13, Issue 1, Page(s) 1950265

    Abstract: Recent recommendations from the European Union Reference Laboratory regarding the generation of antibodies using animals have stimulated significant debate. Here, four of the scientists who served on the Scientific Advisory Committee provide ... ...

    Abstract Recent recommendations from the European Union Reference Laboratory regarding the generation of antibodies using animals have stimulated significant debate. Here, four of the scientists who served on the Scientific Advisory Committee provide clarification of their views regarding the use of animals and
    MeSH term(s) Animal Use Alternatives ; Antibodies ; European Union ; Humans
    Chemical Substances Antibodies
    Language English
    Publishing date 2021-07-20
    Publishing country United States
    Document type Journal Article ; Video-Audio Media
    ZDB-ID 2537838-7
    ISSN 1942-0870 ; 1942-0870
    ISSN (online) 1942-0870
    ISSN 1942-0870
    DOI 10.1080/19420862.2021.1950265
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Primer Design and Inverse PCR on Yeast Display Antibody Selection Outputs.

    Ferrara, Fortunato / Bradbury, Andrew R M / D'Angelo, Sara

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

    2018  Volume 1721, Page(s) 35–45

    Abstract: The display of antibodies on the surface of Saccharomyces cerevisiae cells enables the high-throughput and precise selection of specific binders for the target antigen. The recent implementation of next-generation sequencing (NGS) to antibody display ... ...

    Abstract The display of antibodies on the surface of Saccharomyces cerevisiae cells enables the high-throughput and precise selection of specific binders for the target antigen. The recent implementation of next-generation sequencing (NGS) to antibody display screening provides a complete picture of the entire selected polyclonal population. As such, NGS overcomes the limitations of random clones screening, but it comes with two main limitations: (1) depending upon the platform, the sequencing is usually restricted to the variable heavy chain domain complementary determining region 3 (HCDR3), or VH gene, and does not provide additional information on the rest of the antibody gene, including the VL; and (2) the sequence-identified clones are not physically available for validation. Here, we describe a rapid and effective protocol based on an inverse-PCR method to recover specific antibody clones based on their HCDR3 sequence from a yeast display selection output.
    MeSH term(s) Complementarity Determining Regions/genetics ; DNA Primers/genetics ; Gene Library ; High-Throughput Nucleotide Sequencing ; Polymerase Chain Reaction/methods ; Saccharomyces cerevisiae/genetics ; Single-Chain Antibodies/genetics
    Chemical Substances Complementarity Determining Regions ; DNA Primers ; Single-Chain Antibodies
    Language English
    Publishing date 2018-02-08
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-7546-4_4
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Getting to reproducible antibodies: the rationale for sequenced recombinant characterized reagents.

    Bradbury, Andrew R M / Plückthun, Andreas

    Protein engineering, design & selection : PEDS

    2015  Volume 28, Issue 10, Page(s) 303–305

    MeSH term(s) Animals ; Antibodies/genetics ; Base Sequence ; Indicators and Reagents/metabolism ; Protein Engineering ; Recombinant Proteins/genetics ; Reproducibility of Results
    Chemical Substances Antibodies ; Indicators and Reagents ; Recombinant Proteins
    Language English
    Publishing date 2015-10
    Publishing country England
    Document type Journal Article
    ZDB-ID 1466729-0
    ISSN 1741-0134 ; 1460-213X ; 1741-0126 ; 0269-2139
    ISSN (online) 1741-0134 ; 1460-213X
    ISSN 1741-0126 ; 0269-2139
    DOI 10.1093/protein/gzv051
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  4. Article ; Online: Author Correction: Insights into next generation sequencing guided antibody selection strategies.

    Erasmus, M Frank / Ferrara, Fortunato / D'Angelo, Sara / Spector, Laura / Leal-Lopes, Camila / Teixeira, André A / Sørensen, Jesper / Nagpal, Suhani / Perea-Schmittle, Kathryn / Choudhary, Alok / Honnen, William / Calianese, David / Antonio Rodriguez Carnero, Luis / Cocklin, Simon / Greiff, Victor / Pinter, Abraham / Bradbury, Andrew R M

    Scientific reports

    2024  Volume 14, Issue 1, Page(s) 3090

    Language English
    Publishing date 2024-02-07
    Publishing country England
    Document type Published Erratum
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-024-53751-4
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Animal-free alternatives and the antibody iceberg.

    Gray, Alison / Bradbury, Andrew R M / Knappik, Achim / Plückthun, Andreas / Borrebaeck, Carl A K / Dübel, Stefan

    Nature biotechnology

    2020  Volume 38, Issue 11, Page(s) 1234–1239

    MeSH term(s) Animals ; Antibodies/immunology ; Antibodies, Monoclonal/metabolism ; Immune Sera/metabolism ; Immunity ; Immunization ; Social Control, Formal
    Chemical Substances Antibodies ; Antibodies, Monoclonal ; Immune Sera
    Language English
    Publishing date 2020-10-12
    Publishing country United States
    Document type Letter
    ZDB-ID 1311932-1
    ISSN 1546-1696 ; 1087-0156
    ISSN (online) 1546-1696
    ISSN 1087-0156
    DOI 10.1038/s41587-020-0687-9
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2167: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MO 137: Show issues
    Zs.MG 43: Show issues

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  6. Article ; Online: High throughput purification of monoclonal recombinant antibodies using a Protein-A coated membrane plate system.

    Leal-Lopes, Camila / D'Angelo, Sara / Erasmus, M Frank / Teixeira, Andre A R / Temples, Graham / Zhou, Jinxiang / Bradbury, Andrew R M / Ferrara, Fortunato

    New biotechnology

    2023  Volume 77, Page(s) 111–119

    Abstract: The therapeutic use of monoclonal antibodies (mAbs) ranges from cancer treatment to immune-mediated conditions, covering infectious and cardiovascular disorders, among others. The development of improved methods for therapeutic antibody discovery has ... ...

    Abstract The therapeutic use of monoclonal antibodies (mAbs) ranges from cancer treatment to immune-mediated conditions, covering infectious and cardiovascular disorders, among others. The development of improved methods for therapeutic antibody discovery has accelerated the identification of numerous mAbs: a discovery campaign can be deeply mined, resulting in hundreds, even thousands, of potential antibody leads for a given target of interest. High throughput mAb expression and purification methods are required for the rapid validation of those leads. In this work, we describe the implementation of a Protein-A coated membrane plate system, the Purexa™ AHT membrane plate, for robust preparative purification of hundreds of recombinant mAbs, without the need for automation. The high efficiency (>80%) recovery generated sufficient mAb for downstream screening analyses such as ELISA and surface plasmon resonance (SPR). This new system allows the functional validation of hundreds of lead antibodies from discovery campaigns in a timely manner regardless of operational size.
    MeSH term(s) Antibodies, Monoclonal ; Recombinant Proteins ; Staphylococcal Protein A ; Surface Plasmon Resonance ; Enzyme-Linked Immunosorbent Assay
    Chemical Substances Antibodies, Monoclonal ; Recombinant Proteins ; Staphylococcal Protein A
    Language English
    Publishing date 2023-08-28
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 2400836-9
    ISSN 1876-4347 ; 1876-4347
    ISSN (online) 1876-4347
    ISSN 1876-4347
    DOI 10.1016/j.nbt.2023.08.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Determining the affinities of high-affinity antibodies using KinExA and surface plasmon resonance.

    Erasmus, M Frank / Dovner, Molly / Ferrara, Fortunato / D'Angelo, Sara / Teixeira, André A / Leal-Lopes, Camila / Spector, Laura / Hopkins, Elizabeth / Bradbury, Andrew R M

    mAbs

    2023  Volume 15, Issue 1, Page(s) 2291209

    Abstract: Accurate and efficient affinity measurement techniques are essential for the biophysical characterization of therapeutic monoclonal antibodies, one of the fastest growing drug classes. Surface plasmon resonance (SPR) is widely used for determining ... ...

    Abstract Accurate and efficient affinity measurement techniques are essential for the biophysical characterization of therapeutic monoclonal antibodies, one of the fastest growing drug classes. Surface plasmon resonance (SPR) is widely used for determining antibody affinity, but does not perform well with extremely high affinity (low picomolar to femtomolar range) molecules. In this study, we compare the SPR-based Carterra LSA and the kinetic exclusion assay (KinExA) for measuring the affinities of 48 antibodies generated against the SARS-CoV-2 receptor-binding domain. These data reveal that high-affinity antibodies can be generated straight from selections using high-quality
    MeSH term(s) Surface Plasmon Resonance/methods ; Antibodies, Monoclonal/chemistry ; Antibody Affinity
    Chemical Substances Antibodies, Monoclonal
    Language English
    Publishing date 2023-12-13
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2537838-7
    ISSN 1942-0870 ; 1942-0870
    ISSN (online) 1942-0870
    ISSN 1942-0870
    DOI 10.1080/19420862.2023.2291209
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  8. Article ; Online: Direct selection of functional fluorescent-protein antibody fusions by yeast display.

    Velappan, Nileena / Ferrara, Fortunato / D'Angelo, Sara / Close, Devin / Naranjo, Leslie / Bolding, Madeline R / Mozden, Sarah C / Troup, Camille B / McCullough, Donna K / Gomez, Analyssa / Kedge, Marijo / Bradbury, Andrew R M

    PloS one

    2023  Volume 18, Issue 2, Page(s) e0280930

    Abstract: Antibodies are important reagents for research, diagnostics, and therapeutics. Many examples of chimeric proteins combining the specific target recognition of antibodies with complementing functionalities such as fluorescence, toxicity or enzymatic ... ...

    Abstract Antibodies are important reagents for research, diagnostics, and therapeutics. Many examples of chimeric proteins combining the specific target recognition of antibodies with complementing functionalities such as fluorescence, toxicity or enzymatic activity have been described. However, antibodies selected solely on the basis of their binding specificities are not necessarily ideal candidates for the construction of chimeras. Here, we describe a high throughput method based on yeast display to directly select antibodies most suitable for conversion to fluorescent chimera. A library of scFv binders was converted to a fluorescent chimeric form, by cloning thermal green protein into the linker between VH and VL, and directly selecting for both binding and fluorescent functionality. This allowed us to directly identify antibodies functional in the single chain TGP format, that manifest higher protein expression, easier protein purification, and one-step binding assays.
    MeSH term(s) Saccharomyces cerevisiae/metabolism ; Peptide Library ; Single-Chain Antibodies/genetics ; Antibodies, Monoclonal ; Fluorescent Antibody Technique
    Chemical Substances Peptide Library ; Single-Chain Antibodies ; Antibodies, Monoclonal
    Language English
    Publishing date 2023-02-24
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, N.I.H., Extramural
    ZDB-ID 2267670-3
    ISSN 1932-6203 ; 1932-6203
    ISSN (online) 1932-6203
    ISSN 1932-6203
    DOI 10.1371/journal.pone.0280930
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  9. Article ; Online: The use of phage display in neurobiology.

    Bradbury, Andrew R M

    Current protocols in neuroscience

    2010  Volume Chapter 5, Page(s) Unit 5.12

    Abstract: Phage display has been extensively used to study protein-protein interactions, receptor- and antibody-binding sites, and immune responses, to modify protein properties, and to select antibodies against a wide range of different antigens. In the format ... ...

    Abstract Phage display has been extensively used to study protein-protein interactions, receptor- and antibody-binding sites, and immune responses, to modify protein properties, and to select antibodies against a wide range of different antigens. In the format most often used, a polypeptide is displayed on the surface of a filamentous phage by genetic fusion to one of the coat proteins, creating a chimeric coat protein, and coupling phenotype (the protein) to genotype (the gene within). As the gene encoding the chimeric coat protein is packaged within the phage, selection of the phage on the basis of the binding properties of the polypeptide displayed on the surface simultaneously results in the isolation of the gene encoding the polypeptide. This unit describes the background to the technique, and illustrates how it has been applied to a number of different problems, each of which has its neurobiological counterparts. Although this overview concentrates on the use of filamentous phage, which is the most popular platform, other systems are also described.
    MeSH term(s) Animals ; Antibodies/genetics ; Antibodies/isolation & purification ; Bacteriophages/genetics ; Bacteriophages/immunology ; Bacteriophages/metabolism ; Genes, Viral/genetics ; Genetic Vectors/genetics ; Humans ; Ligands ; Neurobiology/methods ; Peptide Library ; Peptides/genetics ; Peptides/metabolism ; Protein Binding/physiology ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/immunology ; Recombinant Fusion Proteins/metabolism
    Chemical Substances Antibodies ; Ligands ; Peptide Library ; Peptides ; Recombinant Fusion Proteins
    Keywords covid19
    Language English
    Publishing date 2010-04
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 1934-8576
    ISSN (online) 1934-8576
    DOI 10.1002/0471142301.ns0512s51
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  10. Article ; Online: Engineered pH-Sensitive Protein G/IgG Interaction.

    Jha, Ramesh K / Yankey, Allison / Shabazz, Kalifa / Naranjo, Leslie / Shin, Sang-Min / Velappan, Nileena / Bradbury, Andrew R M / Strauss, Charlie E M

    ACS chemical biology

    2021  Volume 16, Issue 7, Page(s) 1142–1146

    Abstract: While natural protein-protein interactions have evolved to be induced by complex stimuli, rational design of interactions that can be switched-on-demand still remain challenging in the protein design world. Here, we demonstrate that a computationally ... ...

    Abstract While natural protein-protein interactions have evolved to be induced by complex stimuli, rational design of interactions that can be switched-on-demand still remain challenging in the protein design world. Here, we demonstrate that a computationally redesigned natural interface for improved binding affinity could further be mutated to adopt a pH switchable interaction. The redesigned interface of Protein G/human IgG Fc domain (referred to as PrG/hIgG), when incorporated with histidine and glutamic acid on PrG (PrG-EHHE), showed a switch in binding affinity by 50-fold when the pH was altered from mild acidic to mild basic. The wild-type (WT) interface showed a negligible switch. The overall binding affinity under mild acidic pH for PrG-EHHE outperformed the wild-type PrG (PrG-WT) interaction. The new reagent PrG-EHHE can be revolutionary in IgG purification, since the standard method of using an extreme acidic pH for elution can be circumvented.
    MeSH term(s) Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Glutamic Acid/chemistry ; Histidine/chemistry ; Humans ; Hydrogen-Ion Concentration ; Immunoglobulin Fc Fragments/chemistry ; Immunoglobulin Fc Fragments/genetics ; Immunoglobulin Fc Fragments/metabolism ; Immunoglobulin G/chemistry ; Immunoglobulin G/metabolism ; Mutation ; Protein Binding ; Protein Domains ; Protein Engineering ; Streptococcus/chemistry
    Chemical Substances Bacterial Proteins ; IgG Fc-binding protein, Streptococcus ; Immunoglobulin Fc Fragments ; Immunoglobulin G ; Glutamic Acid (3KX376GY7L) ; Histidine (4QD397987E)
    Language English
    Publishing date 2021-06-21
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 1554-8937
    ISSN (online) 1554-8937
    DOI 10.1021/acschembio.0c00943
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