ArticleFrontiers in immunology2019
Structural Diversity of Ultralong CDRH3s in Seven Bovine Antibody Heavy Chains.
Article in Frontiers in immunology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 46 citations in OpenAlex.
- Structural Prediction and Antigenic Characterization of Recombinant Nucleocapsid Protein (p14) of Small Ruminant Lentivirus.Viruses · 2026Article
- Comparative Molecular Dynamics Study of 19 Bovine Antibodies with Ultralong CDR H3.Antibodies (Basel, Switzerland) · 2025Article
- The Intrabody Against Murine Double Minute 2 via a p53-Dependent Pathway Induces Apoptosis of Cancer Cell.International journal of molecular sciences · 2025Article
- Bovine Ultra-Long CDR H3 Specific for Bovine Rotavirus Displays Potent Virus Neutralization and Therapeutic Effects in Infected Calves.Biomolecules · 2025Article
- Stability convergence in natural antibodies with ultra-long hypervariable loops.Communications biology · 2025Article
- Annotation of gene loci and analysis of expression diversity in sheep immunoglobulin.Frontiers in immunology · 2025Article
- Analysis of CDR3 region diversity with different lengths in bovine immunoglobulin heavy chain genes.Frontiers in immunology · 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
- Estimates of Sequences with Ultralong and Short CDR3s in the Bovine IgM B Cell Receptor Repertoire Using the Long-read Oxford Nanopore MinION Platform.ImmunoHorizons · 2024Article
- The impact of exchanging the light and heavy chains on the structures of bovine ultralong antibodies.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Modular design of bi- and multi-specific knob domain fusions.Frontiers in immunology · 2024Article
- Conserved antigen structures and antibody-driven variations on foot-and-mouth disease virus serotype A revealed by bovine neutralizing monoclonal antibodies.PLoS pathogens · 2023Article
- The smallest functional antibody fragment: Ultralong CDR H3 antibody knob regions potently neutralize SARS-CoV-2.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Evolution of immunogenetic components encoding ultralong CDR H3.Immunogenetics · 2023Article
- Article
- Serum albumin binding knob domains engineered within a VFrontiers in immunology · 2023Article
- Phage Display of Bovine Ultralong CDRH3.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Germline-Encoded Positional Cysteine Polymorphisms Enhance Diversity in Antibody Ultralong CDR H3 Regions.Journal of immunology (Baltimore, Md. : 1950) · 2022Article
- Variations in antibody repertoires correlate with vaccine responses.Genome research · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antigen recognition by mammalian antibodies represents the most diverse setting for protein-protein interactions, because antibody variable regions contain exceptionally diverse variable gene repertoires of DNA sequences containing combinatorial, non-templated junctional mutational diversity. Some animals use additional strategies to achieve structural complexity in the antibody combining site, and one of the most interesting of these is the formation of ultralong heavy chain complementarity determining region 3 loops in cattle. Repertoire sequencing studies of bovine antibody heavy chain variable sequences revealed that bovine antibodies can contain heavy chain complementarity determining region 3 (CDRH3) loops with 60 or more amino acids, with complex structures stabilized by multiple disulfide bonds. It is clear that bovine antibodies can achieve long, peculiarly structured CDR3s, but the range of diversity and complexity of those structures is poorly understood. We determined the atomic resolution structure of seven ultralong bovine CDRH3 loops. The studies, combined with five previous structures, reveal a large diversity of cysteine pairing variations, and highly diverse globular domains.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.