Di-, tri- and tetrameric single chain Fv antibody fragments against human CD19: Effect of valency on cell binding
Open accessAbstract
Single chain variable fragments (scFv) of the murine monoclonal antibody HD37 specific to human B-cell antigen CD19 were constructed by joining the VH and VL domains with linkers of 18, 10, 1 and 0 residues. ScFv-18 formed monomers, dimers and small amounts of tetramers; scFv-10 formed dimers and small amounts of tetramers; scFv-1 formed exclusively tetramers; scFv-0 formed exclusively trimers. The affinities of the scFv-10 (diabody) and scFv-1 (tetrabody) were approximately 1.5- and 2.5-fold higher, respectively, than that of the scFv-0 (triabody). The tetrabody displayed a significantly prolonged association with cell-bound antigen (t1/2 cell surface retention at 37 degrees C of 26.6 min) compared to both the diabody (13.3 min) and triabody (6.7 min). This increase in avidity of the tetrabody combined with its larger size could prove to be particularly advantageous for imaging and the immunotherapy of B-cell malignancies.
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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 [19]
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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
- Authors
- Le Gall, F., Kipriyanov, S. M., Moldenhauer, G., & Little, M.
- Affiliations
- German Cancer Research Center (DE)
- Corresponding author
- Little, Melvyn
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1999-06-17
- Volume
- 453
- Issue
- 1-2
- Pages
- 164-168
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2017217102
- Cited by
- 128
- References
- 0
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 2 · 2023: 4 · 2022: 3 · 2021: 4 · 2020: 3 · 2019: 3 · 2018: 2 · 2017: 4 · 2016: 3 · 2015: 6 · 2014: 2 · 2013: 4 · 2012: 7
- FWCI
- 7.58
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Commission
- Topics
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Radiopharmaceutical Chemistry and Applications
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
- Keywords
- scFv, diabodies, CD19, B-cell antigens, antibody valency, binding affinity, avidity
- MeSH terms
- Amino Acid Sequence, Antibodies, Monoclonal, Antibody Affinity, Immunoglobulin Fragments, Molecular Sequence Data, Protein Conformation, Recombinant Proteins, Antigens, CD19
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