ArticleImmunology2020
Landscape of variable domain of heavy-chain-only antibody repertoire from alpaca.
Article in Immunology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 25 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
25 citing papers in PubMed, 36 citations in OpenAlex.
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- Species-Dependent Structural Variations in Single-Domain Antibodies.Antibodies (Basel, Switzerland) · 2025Article
- Research Progress on the Application of Neutralizing Nanobodies in the Prevention and Treatment of Viral Infections.Microorganisms · 2025Review
- A synthetic heavy chain variable domain antibody library (VHL) provides highly functional antibodies with favorable developability.Protein science : a publication of the Protein Society · 2025Article
- A Nanobody Toolbox for Recognizing Distinct Epitopes on Cas9.Journal of molecular biology · 2024Article
- NABP-BERT: NANOBODY®-antigen binding prediction based on bidirectional encoder representations from transformers (BERT) architecture.Briefings in bioinformatics · 2024Article
- On the humanization of VHHs: Prospective case studies, experimental and computational characterization of structural determinants for functionality.Protein science : a publication of the Protein Society · 2024Article
- Development, High-Throughput Profiling, and Biopanning of a Large Phage Display Single-Domain Antibody Library.International journal of molecular sciences · 2024Article
- Distinct types of VHHs in Alpaca.Frontiers in immunology · 2024Article
- nanoBERT: a deep learning model for gene agnostic navigation of the nanobody mutational space.Bioinformatics advances · 2024Article
- Development of a bispecific nanobody conjugate broadly neutralizes diverse SARS-CoV-2 variants and structural basis for its broad neutralization.PLoS pathogens · 2023Article
- Nanobodies against C. difficile TcdA and TcdB reveal unexpected neutralizing epitopes and provide a toolkit for toxin quantitation in vivo.PLoS pathogens · 2023Article
- VHH CDR-H3 conformation is determined by VH germline usage.Communications biology · 2023Article
- Fully synthetic platform to rapidly generate tetravalent bispecific nanobody-based immunoglobulins.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Identification of Serum Ferritin-Specific Nanobodies and Development towards a Diagnostic Immunoassay.Biomolecules · 2022Article
- Production and Characterization of Biotinylated Anti-fenitrothion Nanobodies and Development of Sensitive Fluoroimmunoassay.Journal of agricultural and food chemistry · 2022Article
- VInternational journal of molecular sciences · 2022Review
Corrections and comments
- Erratum issuedERRATUM.2022
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Heavy-chain-only antibodies (HCAbs), which are devoid of light chains, have been found naturally occurring in various species including camelids and cartilaginous fish. Because of their high thermostability, refoldability and capacity for cell permeation, the variable regions of the heavy chain of HCAbs (VHHs) have been widely used in diagnosis, bio-imaging, food safety and therapeutics. Most immunogenetic and functional studies of HCAbs are based on case studies or a limited number of low-throughput sequencing data. A complete picture derived from more abundant high-throughput sequencing (HTS) data can help us gain deeper insights. We cloned and sequenced the full-length coding region of VHHs in Alpaca (Vicugna pacos) via HTS in this study. A new pipeline was developed to conduct an in-depth analysis of the HCAb repertoires. Various critical features, including the length distribution of complementarity-determining region 3 (CDR3), V(D)J usage, VJ pairing, germline-specific mutation rate and germline-specific scoring profiles (GSSPs), were systematically characterized. The quantitative data show that V(D)J usage and VHH recombination are highly biased. Interestingly, we found that the average CDR3 length of classical VHHs is longer than that of non-classical ones, whereas the mutation rates are similar in both kinds of VHHs. Finally, GSSPs were built to quantitatively describe and compare sequences that originate from each VJ pair. Overall, this study presents a comprehensive landscape of the HCAb repertoire, which can provide useful guidance for the modeling of somatic hypermutation and the design of novel functional VHHs or VHH repertoires via evolutionary profiles.
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Registered trials
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.