A single-chain variable fragment selected against a conformational epitope of a recombinantly produced snake toxin using phage display
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A single-chain variable fragment selected against a conformational epitope of a recombinantly produced snake toxin using phage display. / Rimbault, Charlotte; Knudsen, Pelle D; Damsbo, Anna; Boddum, Kim; Ali, Hanif; Hackney, Celeste M; Ellgaard, Lars; Bohn, Markus-Frederik; Laustsen, Andreas H.
I: New Biotechnology, Bind 76, 2023, s. 23-32.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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T1 - A single-chain variable fragment selected against a conformational epitope of a recombinantly produced snake toxin using phage display
AU - Rimbault, Charlotte
AU - Knudsen, Pelle D
AU - Damsbo, Anna
AU - Boddum, Kim
AU - Ali, Hanif
AU - Hackney, Celeste M
AU - Ellgaard, Lars
AU - Bohn, Markus-Frederik
AU - Laustsen, Andreas H
N1 - Copyright © 2023. Published by Elsevier B.V.
PY - 2023
Y1 - 2023
N2 - Phage display technology is a powerful tool for selecting monoclonal antibodies against a diverse set of antigens. Within toxinology, however, it remains challenging to generate monoclonal antibodies against many animal toxins, as they are difficult to obtain from venom. Recombinant toxins have been proposed as a solution to overcome this challenge, but so far, few have been used as antigens to generate neutralizing antibodies. Here, we describe the recombinant expression of α-cobratoxin in E. coli and its successful application as an antigen in a phage display selection campaign. From this campaign, an scFv (single chain variable fragment) was isolated with similar binding affinity to a control scFv generated against the native toxin. The selected scFv recognizes a structural epitope, enabling it to inhibit the interaction between the acetylcholine receptor and the native toxin in vitro. This approach represents the first entirely in vitro antibody selection strategy for generating neutralizing monoclonal antibodies against a snake toxin.
AB - Phage display technology is a powerful tool for selecting monoclonal antibodies against a diverse set of antigens. Within toxinology, however, it remains challenging to generate monoclonal antibodies against many animal toxins, as they are difficult to obtain from venom. Recombinant toxins have been proposed as a solution to overcome this challenge, but so far, few have been used as antigens to generate neutralizing antibodies. Here, we describe the recombinant expression of α-cobratoxin in E. coli and its successful application as an antigen in a phage display selection campaign. From this campaign, an scFv (single chain variable fragment) was isolated with similar binding affinity to a control scFv generated against the native toxin. The selected scFv recognizes a structural epitope, enabling it to inhibit the interaction between the acetylcholine receptor and the native toxin in vitro. This approach represents the first entirely in vitro antibody selection strategy for generating neutralizing monoclonal antibodies against a snake toxin.
U2 - 10.1016/j.nbt.2023.04.002
DO - 10.1016/j.nbt.2023.04.002
M3 - Journal article
C2 - 37037303
VL - 76
SP - 23
EP - 32
JO - New Biotechnology
JF - New Biotechnology
SN - 1871-6784
ER -
ID: 342678615