ArticlePloS one2013
Contributions of the complementarity determining regions to the thermal stability of a single-domain antibody.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 citing papers in PubMed, 38 citations in OpenAlex.
- Multidimensional maturation of antibody variable domains with machine-learning assistance.mAbs · 2026Article
- Hypervariable loop profiling decodes sequence determinants of antibody stability.Nature structural & molecular biology · 2026Article
- 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
- Screening of Pancreatic Ribonuclease A Inhibitors from an Autodisplayed Fv-Antibody Library.ACS pharmacology & translational science · 2023Article
- NbThermo: a new thermostability database for nanobodies.Database : the journal of biological databases and curation · 2023Article
- Increasing the melting temperature of VHH with the in silico free energy score.Scientific reports · 2023Article
- Unveiling the affinity-stability relationship in anti-measles virus antibodies: a computational approach for hotspots prediction.Frontiers in molecular biosciences · 2023Article
- Molecular basis for thermal stability and affinity in a VHH: Contribution of the framework region and its influence in the conformation of the CDR3.Protein science : a publication of the Protein Society · 2022Article
- Co-optimization of therapeutic antibody affinity and specificity using machine learning models that generalize to novel mutational space.Nature communications · 2022Article
- Structural Insights into the Design of Synthetic Nanobody Libraries.Molecules (Basel, Switzerland) · 2022Review
- Delicate balance among thermal stability, binding affinity, and conformational space explored by single-domain VScientific reports · 2021Article
- Protein design and variant prediction using autoregressive generative models.Nature communications · 2021Article
- Generation of synthetic nanobodies against delicate proteins.Nature protocols · 2020Article
- Experimental evaluation of single-domain antibodies predicted by molecular dynamics simulations to have elevated thermal stability.Protein science : a publication of the Protein Society · 2019Article
- Domain swapping of complementarity-determining region in nanobodies produced by Pichia pastoris.AMB Express · 2019Article
- Sequence Tolerance of a Single-Domain Antibody with a High Thermal Stability: Comparison of Computational and Experimental Fitness Profiles.ACS omega · 2019Article
- Understanding and overcoming trade-offs between antibody affinity, specificity, stability and solubility.Biochemical engineering journal · 2018Article
- Article
- Enhancing Stability of Camelid and Shark Single Domain Antibodies: An Overview.Frontiers in immunology · 2017Review
- Molecular dynamics simulations and docking enable to explore the biophysical factors controlling the yields of engineered nanobodies.Scientific reports · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Single domain antibodies (sdAbs) are the recombinantly-expressed variable domain from camelid (or shark) heavy chain only antibodies and provide rugged recognition elements. Many sdAbs possess excellent affinity and specificity; most refold and are able to bind antigen after thermal denaturation. The sdAb A3, specific for the toxin Staphylococcal enterotoxin B (SEB), shows both sub-nanomolar affinity for its cognate antigen (0.14 nM) and an unusually high melting point of 85°C. Understanding the source of sdAb A3's high melting temperature could provide a route for engineering improved melting temperatures into other sdAbs. The goal of this work was to determine how much of sdAb A3's stability is derived from its complementarity determining regions (CDRs) versus its framework. Towards answering this question we constructed a series of CDR swap mutants in which the CDRs from unrelated sdAbs were integrated into A3's framework and where A3's CDRs were integrated into the framework of the other sdAbs. All three CDRs from A3 were moved to the frameworks of sdAb D1 (a ricin binder that melts at 50°C) and the anti-ricin sdAb C8 (melting point of 60°C). Similarly, the CDRs from sdAb D1 and sdAb C8 were moved to the sdAb A3 framework. In addition individual CDRs of sdAb A3 and sdAb D1 were swapped. Melting temperature and binding ability were assessed for each of the CDR-exchange mutants. This work showed that CDR2 plays a critical role in sdAb A3's binding and stability. Overall, results from the CDR swaps indicate CDR interactions play a major role in the protein stability.
Indexed as
Identifiers
What OpenQuestion holds
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.