A single-chain variable fragment selected against a conformational epitope of a recombinantly produced snake toxin using phage display

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Standard

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

Harvard

Rimbault, C, Knudsen, PD, Damsbo, A, Boddum, K, Ali, H, Hackney, CM, Ellgaard, L, Bohn, M-F & Laustsen, AH 2023, 'A single-chain variable fragment selected against a conformational epitope of a recombinantly produced snake toxin using phage display', New Biotechnology, bind 76, s. 23-32. https://doi.org/10.1016/j.nbt.2023.04.002

APA

Rimbault, C., Knudsen, P. D., Damsbo, A., Boddum, K., Ali, H., Hackney, C. M., Ellgaard, L., Bohn, M-F., & Laustsen, A. H. (2023). A single-chain variable fragment selected against a conformational epitope of a recombinantly produced snake toxin using phage display. New Biotechnology, 76, 23-32. https://doi.org/10.1016/j.nbt.2023.04.002

Vancouver

Rimbault C, Knudsen PD, Damsbo A, Boddum K, Ali H, Hackney CM o.a. A single-chain variable fragment selected against a conformational epitope of a recombinantly produced snake toxin using phage display. New Biotechnology. 2023;76:23-32. https://doi.org/10.1016/j.nbt.2023.04.002

Author

Rimbault, Charlotte ; Knudsen, Pelle D ; Damsbo, Anna ; Boddum, Kim ; Ali, Hanif ; Hackney, Celeste M ; Ellgaard, Lars ; Bohn, Markus-Frederik ; Laustsen, Andreas H. / A single-chain variable fragment selected against a conformational epitope of a recombinantly produced snake toxin using phage display. I: New Biotechnology. 2023 ; Bind 76. s. 23-32.

Bibtex

@article{1b9d42e1ce5f4377b8096542d6df2d83,

title = "A single-chain variable fragment selected against a conformational epitope of a recombinantly produced snake toxin using phage display",

abstract = "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.",

author = "Charlotte Rimbault and Knudsen, {Pelle D} and Anna Damsbo and Kim Boddum and Hanif Ali and Hackney, {Celeste M} and Lars Ellgaard and Markus-Frederik Bohn and Laustsen, {Andreas H}",

note = "Copyright {\textcopyright} 2023. Published by Elsevier B.V.",

year = "2023",

doi = "10.1016/j.nbt.2023.04.002",

language = "English",

volume = "76",

pages = "23--32",

journal = "New Biotechnology",

issn = "1871-6784",

publisher = "Elsevier",

}

RIS

TY - JOUR

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

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

Biologisk Institut