Replacing the complementarity-determining regions in a human antibody with those from a mouse
Abstract
The variable domains of an antibody consist of a beta-sheet framework with hypervariable regions (or complementarity-determining regions--CDRs) which fashion the antigen-binding site. Here we attempted to determine whether the antigen-binding site could be transplanted from one framework to another by grafting the CDRs. We substituted the CDRs from the heavy-chain variable region of mouse antibody B1-8, which binds the hapten NP-cap (4-hydroxy-3-nitrophenacetyl caproic acid; KNP-cap = 1.2 microM), for the corresponding CDRs of a human myeloma protein. We report that in combination with the B1-8 mouse light chain, the new antibody has acquired the hapten affinity of the B1-8 antibody (KNP-cap = 1.9 microM). Such 'CDR replacement' may offer a means of constructing human monoclonal antibodies from the corresponding mouse monoclonal antibodies.
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Animal-derived antibodies undergo humanization to avoid immunological issues.
“To avoid such issues, animal-derived antibodies undergo a process called humanization [185, 186].”
From Computational approaches to therapeutic antibody design: established methods and emerging trends (2020) · cites this paper as [185]
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References 29 · Cited by 1,406
- Authors
- Jones, P. T., Dear, P. H., Foote, J., Neuberger, M. S., & Winter, G.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Venue
- Nature
- Published
- 1986-05
- Volume
- 321
- Issue
- 6069
- Pages
- 522-525
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2075097399
- Cited by
- 1,406
- References
- 29
- Citations by year
- 2026: 19 · 2025: 48 · 2024: 33 · 2023: 29 · 2022: 33 · 2021: 43 · 2020: 40 · 2019: 30 · 2018: 40 · 2017: 36 · 2016: 33 · 2015: 45 · 2014: 32 · 2013: 52 · 2012: 52
- FWCI
- 31.66
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Keywords
- hypervariable region, immunoglobulin variable region, framework regions, antibody binding sites, myeloma proteins
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Genes, Humans, Immunoglobulin E, Immunoglobulin Variable Region, Models, Molecular, Myeloma Proteins, Plasmids, Protein Conformation, Species Specificity, Mice
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