Evidence map›Paper›PMID 34795299›Full record

ArticleNature communications2021

Mechanistic principles of an ultra-long bovine CDR reveal strategies for antibody design.

Hristo L Svilenov, Julia Sacherl, Ulrike Protzer, Martin Zacharias, Johannes Buchner

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

14 citing papers in PubMed, 29 citations in OpenAlex.

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  11. The impact of exchanging the light and heavy chains on the structures of bovine ultralong antibodies.Acta crystallographica. Section F, Structural biology communications · 2024
    Article
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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

5 authors at 2 institutions in 1 country.

Hristo L SvilenovCenter for Protein Assemblies and Department Chemie, Technische Universität München, 85748, Garching, Germany. hristo.svilenov@tum.de.ORCID http://orcid.org/0000-0001-5863-9569
Julia SacherlInstitute of Virology, Technical University of Munich / Helmholtz Zentrum Munich, Munich, Germany.
Ulrike ProtzerInstitute of Virology, Technical University of Munich / Helmholtz Zentrum Munich, Munich, Germany.ORCID http://orcid.org/0000-0002-9421-1911
Martin ZachariasCenter for Protein Assemblies and the Department Physik, Technische Universität München, 85748, Garching, Germany.
Johannes BuchnerCenter for Protein Assemblies and Department Chemie, Technische Universität München, 85748, Garching, Germany. johannes.buchner@tum.de.ORCID http://orcid.org/0000-0003-1282-7737
Center for Integrated Protein Science Munich · DEHelmholtz Zentrum München · DE

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) BU 836/6-3
6 · The paper itself

Abstract

Antibodies bind antigens via flexible loops called complementarity-determining regions (CDRs). These are usually 6-20 residues long. However, some bovine antibodies have ultra-long CDRs comprising more than 50 residues organized in a stalk and a disulfide-rich knob. The design features of this structural unit and its influence on antibody stability remained enigmatic. Here, we show that the stalk length is critical for the folding and stability of antibodies with an ultra-long CDR and that the disulfide bonds in the knob do not contribute to stability; they are important for organizing the antigen-binding knob structure. The bovine ultra-long CDR can be integrated into human antibody scaffolds. Furthermore, mini-domains from de novo design can be reformatted as ultra-long CDRs to create unique antibody-based proteins neutralizing SARS-CoV-2 and the Alpha variant of concern with high efficiency. Our findings reveal basic design principles of antibody structure and open new avenues for protein engineering.

Indexed as

AnimalsAntibodies, ViralCattleComplementarity Determining RegionsCOVID-19SARS-CoV-2Antibodies, ViralComplementarity Determining Regions

Identifiers

PMID34795299
PMCPMC8602281
OpenAlexW3213441803

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.