ArticleCommunications biology2025
Stability convergence in natural antibodies with ultra-long hypervariable loops.
Article in Communications biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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Who cites it
4 citing papers in PubMed.
- Phage Display Technology: Design, Library Construction, and Panning Strategies for Antibody Development.Biomolecules & therapeutics · 2026Review
- Class switched bovine ultralong CDR H3 amplicons versus canonical in immune and non-immune tissues.Immunogenetics · 2026Article
- Selection and evaluation of new sites for splitting beta-lactamase to modulate auto-complementation enzyme activity.Biochimica et biophysica acta. General subjects · 2026Article
- Therapeutic efficacy of bovine ultra-long CDR H3 antibody against BVDV in challenged BALB/c mouse model.Frontiers in immunology · 2026Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Antibodies bind to antigens with hypervariable loops called complementarity-determining regions (CDRs). In contrast to conventional antibodies, a subset of bovine antibodies has an ultra-long CDR (ulCDR) composed of up to 70 residues folded as a stalk and knob. The fundamental principles of how these antibodies maintain their structure and stability remain enigmatic. Here, we investigated how different natural ulCDRs affect antibody structure, stability and function. To this end, we swapped diverse ulCDRs onto the same antibody scaffold. All ulCDR-swap variants exhibit nearly identical secondary structure fingerprints and remarkably similar thermal stability. In addition, specificity and high-affinity binding to the antigens are maintained. Hydrogen-deuterium exchange and molecular dynamics simulations suggest small differences between the variants arising from changed interactions between different stalks and the underlying scaffold. Overall, we reveal principles of grafting natural ulCDRs onto a common Fab scaffold, which have implications for antibody design for biomedical applications.
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Registered trials
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