Evidence map›Paper›PMID 37876265›Full record

ArticlemAbs

A window into the human immune system: comprehensive characterization of the complexity of antibody complementary-determining regions in functional antibodies.

Oscar Mejias-Gomez, Andreas V Madsen, Kerstin Skovgaard, Lasse E Pedersen, J Preben Morth, Timothy P Jenkins, Peter Kristensen, Steffen Goletz

Open access · goldAbstract read
In one paragraph

Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
6.0field-weighted citation impact, top 3% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 26 citations in OpenAlex.

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  6. Data-optimal scaling of paired antibody language models.bioRxiv : the preprint server for biology · 2025
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Oscar Mejias-GomezDepartment of Biotechnology and Biomedicine, Technical University of Denmark, Kgs. Lyngby, Denmark.ORCID 0000-0002-1026-6692
Andreas V MadsenDepartment of Biotechnology and Biomedicine, Technical University of Denmark, Kgs. Lyngby, Denmark.ORCID 0000-0002-8449-9691
Kerstin SkovgaardDepartment of Biotechnology and Biomedicine, Technical University of Denmark, Kgs. Lyngby, Denmark.ORCID 0000-0001-5663-4879
Lasse E PedersenDepartment of Biotechnology and Biomedicine, Technical University of Denmark, Kgs. Lyngby, Denmark.ORCID 0000-0002-6064-919X
J Preben MorthDepartment of Biotechnology and Biomedicine, Technical University of Denmark, Kgs. Lyngby, Denmark.ORCID 0000-0003-4077-0192
Timothy P JenkinsDepartment of Biotechnology and Biomedicine, Technical University of Denmark, Kgs. Lyngby, Denmark.ORCID 0000-0003-2979-5663
Peter KristensenDepartment of Chemistry and Bioscience, Aalborg University, Aalborg, Denmark.ORCID 0000-0001-7205-6853
Steffen GoletzDepartment of Biotechnology and Biomedicine, Technical University of Denmark, Kgs. Lyngby, Denmark.ORCID 0000-0003-1463-5448
Technical University of Denmark · DKAalborg University · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human immune system uses antibodies to neutralize foreign antigens. They are composed of heavy and light chains, both with constant and variable regions. The variable region has six hypervariable loops, also known as complementary-determining regions (CDRs) that determine antibody diversity and antigen specificity. Knowledge of their significance, and certain residues present in these areas, is vital for antibody therapeutics development. This study includes an analysis of more than 11,000 human antibody sequences from the International Immunogenetics information system (IMGT). The analysis included parameters such as length distribution, overall amino acid diversity, amino acid frequency per CDR and residue position within antibody chains. Overall, our findings confirm existing knowledge, such as CDRH3's high length diversity and amino acid variability, increased aromatic residue usage, particularly tyrosine, charged and polar residues like aspartic acid, serine, and the flexible residue glycine. Specific residue positions within each CDR influence these occurrences, implying a unique amino acid type distribution pattern. We compared amino acid type usage in CDRs and non-CDR regions, both in globular and transmembrane proteins, which revealed distinguishing features, such as increased frequency of tyrosine, serine, aspartic acid, and arginine. These findings should prove useful for future optimization, improvement of affinity, synthetic antibody library design, or the creation of antibodies

Indexed as

AntibodiesAspartic AcidAmino Acid SequenceComplementarity Determining RegionsHumansImmune SystemSerineTyrosineAntibodiesAspartic AcidComplementarity Determining RegionsSerineTyrosineAmino acid diversityantibodies/immunoglobulinsantibody-antigen complexesantibody sequencingantibody therapeutics developmentComplementary-Determining Regions (CDRs)de-novo in silico antibody designIMGT (International Immunogenetics Information System)immunologysynthetic antibody libraries

Identifiers

PMID37876265
PMCPMC10601506
OpenAlexW4387930602

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.