ArticlemAbs2020
Potent neutralization of SARS-CoV-2 by human antibody heavy-chain variable domains isolated from a large library with a new stable scaffold.
Article in mAbs, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 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
43 citing papers in PubMed, 64 citations in OpenAlex.
- Clinical sensitivity and interpretation of PCR and serological COVID-19 diagnostics for patients presenting to the hospital.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Trial
- 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
- Engineering a "muco-trapping" ACE2-immunoglobulin hybrid with picomolar affinity as an inhaled, pan-variant immunotherapy for COVID-19.Bioengineering & translational medicine · 2024Article
- Identification of a Fully Human Antibody VH Domain Targeting Anaplastic Lymphoma Kinase (ALK) with Applications in ALK-Positive Solid Tumor Immunotherapy.Antibodies (Basel, Switzerland) · 2024Article
- Preclinical assessment of a novel human antibody VH domain targeting mesothelin as an antibody-drug conjugate.Molecular therapy oncolytics · 2023Article
- Assessment of Novel Mesothelin-Specific Human Antibody Domain VH-Fc Fusion Proteins-Based PET Agents.ACS omega · 2023Article
- Literature-Based Discovery to Elucidate the Biological Links between Resistant Hypertension and COVID-19.Biology · 2023Article
- Clinical Application of Antibody Immunity Against SARS-CoV-2: Comprehensive Review on Immunoassay and Immunotherapy.Clinical reviews in allergy & immunology · 2023Review
- Human antibody VFrontiers in oncology · 2023Article
- Avidity engineering of human heavy-chain-only antibodies mitigates neutralization resistance of SARS-CoV-2 variants.Frontiers in immunology · 2023Article
- Article
- SARS-CoV-2 variants of concern: spike protein mutational analysis and epitope for broad neutralization.Nature communications · 2022Article
- Correlation between the binding affinity and the conformational entropy of nanobody SARS-CoV-2 spike protein complexes.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Animal models for COVID-19: advances, gaps and perspectives.Signal transduction and targeted therapy · 2022Review
- A SARS-CoV-2 nanobody that can bind to the RBD region may be used for treatment in COVID-19 in animals.Research in veterinary science · 2022Article
- Potent Neutralization of Omicron and other SARS-CoV-2 Variants of Concern by Biparatopic Human VH Domains.bioRxiv : the preprint server for biology · 2022Article
- A Detailed Overview of Immune Escape, Antibody Escape, Partial Vaccine Escape of SARS-CoV-2 and Their Emerging Variants With Escape Mutations.Frontiers in immunology · 2022Review
- A humanized nanobody phage display library yields potent binders of SARS CoV-2 spike.PloS one · 2022Article
- Construction of a Large Size Human Immunoglobulin Heavy Chain Variable (VH) Domain Library, Isolation and Characterization of Novel Human Antibody VH Domains Targeting PD-L1 and CD22.Frontiers in immunology · 2022Article
- Generation and utility of a single-chain fragment variable monoclonal antibody platform against a baculovirus expressed recombinant receptor binding domain of SARS-CoV-2 spike protein.Molecular immunology · 2022Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
Abstract
Effective therapies are urgently needed for COVID-19. Here we describe the identification of a new stable human immunoglobulin G1 heavy-chain variable (VH) domain scaffold that was used for the construction of a large library, lCAT6, of engineered human VHs. This library was panned against the receptor-binding domain (RBD) of the SARS-CoV-2 spike (S) glycoprotein. Two VH domains (VH ab6 and VH m397) were selected and fused to Fc for increased half-life in circulation. The VH-Fc ab6 and m397 specifically neutralized SARS-CoV-2 with high potencies (50% neutralization at 0.35 µg/ml and 1.5 µg/ml, respectively) as measured by two independent replication-competent virus neutralization assays. Ab6 and m397 competed with ACE2 for binding to RBD, suggesting a competitive mechanism of virus neutralization. These VH domains may have potential applications for prophylaxis and therapy of COVID-19 alone or in combination, as well as for diagnosis and as tools for research.
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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.