ArticleAntibodies (Basel, Switzerland)2024
50 Years of Antibody Numbering Schemes: A Statistical and Structural Evaluation Reveals Key Differences and Limitations.
Article in Antibodies (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Potent neutralization of Rift Valley fever virus mediated by monoclonal antibodies via concurrent inhibition of attachment and fusion.Emerging microbes & infections · 2026Article
- Adaptive Disorder as the Hallmark of Nanobodies Antigen-Binding Loops.Journal of chemical information and modeling · 2026Article
- Revised Adaptive Immune Receptor Data in the Immune Epitope Database.bioRxiv : the preprint server for biology · 2026Article
- Antibody numbering schemes: advances, comparisons and tools for antibody engineering.Protein engineering, design & selection : PEDS · 2025Review
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Authors and funding
3 authors.
Funding
Abstract
backgroundThe complementarity-determining region (CDR) of antibodies represents the most diverse region both in terms of sequence and structural characteristics, playing the most critical role in antibody recognition and binding for immune responses. Over the past decades, several numbering schemes have been introduced to define CDRs based on sequence. However, the existence of diverse numbering schemes has led to potential confusion, and a comprehensive evaluation of these schemes is lacking.
methodsWe employ statistical analyses to quantify the diversity of CDRs compared to the framework regions.
resultsComparative analyses across different numbering schemes demonstrate notable variations in CDR definitions. The Kabat and AbM numbering schemes tend to incorporate more conserved residues into their CDR definitions, whereas CDRs defined by the Chothia and IMGT numbering schemes display greater diversity, sometimes missing certain loop residues. Notably, we identify a critical residue, L29, within the kappa light chain CDR1, which appears to act as a pivotal structural point within the loop. In contrast, most numbering schemes designate the topological equivalent point in the lambda light chain as L30, suggesting the need for further refinement in the current numbering schemes.
conclusionsThese findings shed light on regional sequence and structural conservation within antibody sequence databases while also highlighting discrepancies stemming from different numbering schemes. These insights yield valuable guidelines for the precise delineation of antibody CDRs and the strategic design of antibody repertoires, with practical implications in developing innovative antibody-based therapeutics and diagnostics.
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