Triabodies: Single chain Fv fragments without a linker form trivalent trimers
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A single chain Fv fragment (scFv) of the murine monoclonal antibody 11‐1G10 was constructed by directly joining the C‐terminal residue of the V H domain to the N‐terminal residue of V L. 11‐1G10 is an anti‐idiotype and competes with the antigen, influenza virus neuraminidase (NA), for binding to the NC41 antibody. The scFv formed stable trimers with three active antigen combining sites for NC41 Fab fragments. We propose that trimeric scFvs may be the preferred conformation for directly linked V H‐V L molecules, which contrasts the formation of scFv dimers (diabodies) when the V H and V L domains are joined by short flexible linkers of between 5–10 residues. BIAcore biosensor binding experiments showed that the trimeric scFv showed an expected increase in binding affinity, due to avidity, compared to the monomeric 15‐residue linked scFv. The increase in avidity of scFv trimers offers advantages for imaging and immunotherapy.
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Linker length influences oligomeric state: linkers greater than 15 residues generally lead to monomers, linkers of 6-15 residues can favor stable dimers and trimers, and linkers with fewer than five residues result in higher-order multimeric molecules.
“It has been largely demonstrated that the linker length influences the oligomeric state. Linkers greater than 15 residues generally lead to monomers while linkers of 6–15 residues can be utilized to deliberately favor the formation of stable dimers and trimers [17,18]. Linkers with fewer than five residues result in the generation of higher-order multimeric molecules [19,20].”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [18]
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Research works printed but not linked: 6
- Zdanov, A., Li, Y., Bundle, D.R., Deng, S.-J., MacKenzie, C.R., Narang, S.A., Young, N.M., Cygler, M., Proc. Natl. Acad. Sei. USA 91 (1994) 6423-6427.
- Holliger, P., Prospero, T., Winter, G., Proc. Natl. Acad. Sei. USA 90 (1993) 6444-6448. [9: [10[
- Hudson, P.J., in: Monoclonal Antibodies: The Second Genera- tion (H. Zola, Ed.), BIOS Scientific Publications, Oxford, UK, 1995, pp. 183-202.
- Kortt, A.A., Lah, M., Oddie, G.W., Gruen, L.C., Burns, J.E., Pearce, L.A., Atwell, J.L., McCoy, A.J., Howlett, G.J., Metzger, D.W., Webster, R.G., Hudson, P.J., Protein Eng. 1997 (in press).
- Metzger, D.W., Webster, R.G., in: Idiotype Networks in Biology and Medicine (Osterhaus, A.D.M.E. and Uytdellaag, F.G.C.M., Eds.), Elsevier, Amsterdam/New York, 1996, pp. 257-267.
- Kortt, A.A., Gruen, L.C., Oddie, G.W., J. Mol. Recognit. 1997 (in press).
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Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments
Sandomenico, A., Sivaccumar, J. P., & Ruvo, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176324 · Cited by 134 · see citing works
Orientation of antigen binding sites in dimeric and trimeric single chain Fv antibody fragments
Lawrence, L. J., Kortt, A. A., Iliades, P., Tulloch, P. A., & Hudson, P. J. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00292-0 · Cited by 50 · see citing works
Self-citation
- Authors
- Iliades, P., Kortt, A. A., & Hudson, P. J.
- Affiliations
- Commonwealth Scientific and Industrial Research Organisation (AU)
- Corresponding author
- Hudson, Peter J
- ORCID
- Hudson, Peter J
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1997-06-16
- Volume
- 409
- Issue
- 3
- Pages
- 437-441
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2010039421
- Cited by
- 110
- References
- 0
- Citations by year
- 2025: 1 · 2024: 2 · 2023: 1 · 2022: 2 · 2020: 2 · 2019: 1 · 2018: 1 · 2016: 3 · 2015: 3 · 2013: 1 · 2012: 3
- FWCI
- 12.02
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Commonwealth Scientific and Industrial Research Organisation
- Topics
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- single-chain Fv fragments, anti-idiotypic antibodies, influenza neuraminidase, diabodies, avidity, binding affinity, antibody conformation, immunotherapy
- MeSH terms
- Animals, Antibodies, Monoclonal, Binding Sites, Antibody, Biopolymers, Chromatography, Gel, Immunoglobulin Fragments, Immunoglobulin Variable Region, Immunoglobulin Heavy Chains, Immunoglobulin Light Chains, Ligands, Orthomyxoviridae, Solutions, HN Protein, Mice
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