ArticleActa crystallographica. Section F, Structural biology communications2024
The impact of exchanging the light and heavy chains on the structures of bovine ultralong antibodies.
Article in Acta crystallographica. Section F, Structural biology communications, 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.
- Comparative Molecular Dynamics Study of 19 Bovine Antibodies with Ultralong CDR H3.Antibodies (Basel, Switzerland) · 2025Article
- Stability convergence in natural antibodies with ultra-long hypervariable loops.Communications biology · 2025Article
- Investigating the IgM and IgG B Cell Receptor Repertoires and Expression of Ultralong Complementarity Determining Region 3 in Colostrum and Blood from Holstein-Friesian Cows at Calving.Animals : an open access journal from MDPI · 2024Article
- A broadly reactive ultralong bovine antibody that can determine the integrity of foot-and-mouth disease virus capsids.The Journal of general virology · 2024Article
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Authors and funding
9 authors.
Funding
Abstract
The third complementary-determining regions of the heavy-chain (CDR3H) variable regions (VH) of some cattle antibodies are highly extended, consisting of 48 or more residues. These `ultralong' CDR3Hs form β-ribbon stalks that protrude from the surface of the antibody with a disulfide cross-linked knob region at their apex that dominates antigen interactions over the other CDR loops. The structure of the Fab fragment of a naturally paired bovine ultralong antibody (D08), identified by single B-cell sequencing, has been determined to 1.6 Å resolution. By swapping the D08 native light chain with that of an unrelated antigen-unknown ultralong antibody, it is shown that interactions between the CDR3s of the variable domains potentially affect the fine positioning of the ultralong CDR3H; however, comparison with other crystallographic structures shows that crystalline packing is also a major contributor. It is concluded that, on balance, the exact positioning of ultralong CDR3H loops is most likely to be due to the constraints of crystal packing.
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