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Humanization of chicken‐derived scFv using yeast surface display and NGS data mining

Elter, Adrian ; Bogen, Jan P. ; Hinz, Steffen C. ; Fiebig, David ; Macarrón Palacios, Arturo ; Grzeschik, Julius ; Hock, Björn ; Kolmar, Harald (2021)
Humanization of chicken‐derived scFv using yeast surface display and NGS data mining.
In: Biotechnology Journal : Systems & Synthetic Biology, Nanobiotech, Medicine, 16 (3)
doi: 10.1002/biot.202000231
Artikel, Bibliographie

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Kurzbeschreibung (Abstract)

Generation of high‐affinity monoclonal antibodies by immunization of chickens is a valuable strategy, particularly for obtaining antibodies directed against epitopes that are conserved in mammals. A generic procedure is established for the humanization of chicken‐derived antibodies. To this end, high‐affinity binders of the epidermal growth factor receptor extracellular domain are isolated from immunized chickens using yeast surface display. Complementarity determining regions (CDRs) of two high‐affinity binders are grafted onto a human acceptor framework. Simultaneously, Vernier zone residues, responsible for spatial CDR arrangement, are partially randomized. A yeast surface display library comprising ≈300 000 variants is screened for high‐affinity binders in the scFv and Fab formats. Next‐generation sequencing discloses humanized antibody variants with restored affinity and improved protein characteristics compared to the parental chicken antibodies. Furthermore, the sequencing data give new insights into the importance of antibody format, used during the humanization process. Starting from the antibody repertoire of immunized chickens, this work features an effective and fast high‐throughput approach for the generation of multiple humanized antibodies with potential therapeutic relevance.

Typ des Eintrags: Artikel
Erschienen: 2021
Autor(en): Elter, Adrian ; Bogen, Jan P. ; Hinz, Steffen C. ; Fiebig, David ; Macarrón Palacios, Arturo ; Grzeschik, Julius ; Hock, Björn ; Kolmar, Harald
Art des Eintrags: Bibliographie
Titel: Humanization of chicken‐derived scFv using yeast surface display and NGS data mining
Sprache: Englisch
Publikationsjahr: 2021
Ort: Weinheim
Verlag: Wiley-VCH
Titel der Zeitschrift, Zeitung oder Schriftenreihe: Biotechnology Journal : Systems & Synthetic Biology, Nanobiotech, Medicine
Jahrgang/Volume einer Zeitschrift: 16
(Heft-)Nummer: 3
Kollation: 9 Seiten
DOI: 10.1002/biot.202000231
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Kurzbeschreibung (Abstract):

Generation of high‐affinity monoclonal antibodies by immunization of chickens is a valuable strategy, particularly for obtaining antibodies directed against epitopes that are conserved in mammals. A generic procedure is established for the humanization of chicken‐derived antibodies. To this end, high‐affinity binders of the epidermal growth factor receptor extracellular domain are isolated from immunized chickens using yeast surface display. Complementarity determining regions (CDRs) of two high‐affinity binders are grafted onto a human acceptor framework. Simultaneously, Vernier zone residues, responsible for spatial CDR arrangement, are partially randomized. A yeast surface display library comprising ≈300 000 variants is screened for high‐affinity binders in the scFv and Fab formats. Next‐generation sequencing discloses humanized antibody variants with restored affinity and improved protein characteristics compared to the parental chicken antibodies. Furthermore, the sequencing data give new insights into the importance of antibody format, used during the humanization process. Starting from the antibody repertoire of immunized chickens, this work features an effective and fast high‐throughput approach for the generation of multiple humanized antibodies with potential therapeutic relevance.

Freie Schlagworte: chicken antibody, fluorescence‐activated cell sorting, humanization, next‐generation sequencing, yeast surface display
ID-Nummer: Artikel-ID: 2000231
Sachgruppe der Dewey Dezimalklassifikatin (DDC): 500 Naturwissenschaften und Mathematik > 540 Chemie
500 Naturwissenschaften und Mathematik > 570 Biowissenschaften, Biologie
Fachbereich(e)/-gebiet(e): 07 Fachbereich Chemie
07 Fachbereich Chemie > Clemens-Schöpf-Institut > Fachgebiet Biochemie
07 Fachbereich Chemie > Clemens-Schöpf-Institut
Hinterlegungsdatum: 13 Feb 2024 07:37
Letzte Änderung: 13 Feb 2024 07:38
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