Evidence map›Paper›PMID 35547740›Full record

ArticleFrontiers in immunology2022

Nanobodies Protecting From Lethal SARS-CoV-2 Infection Target Receptor Binding Epitopes Preserved in Virus Variants Other Than Omicron.

José M Casasnovas, Yago Margolles, María A Noriega, María Guzmán, Rocío Arranz, Roberto Melero, Mercedes Casanova, Juan Alberto Corbera, Nereida Jiménez-de-Oya, Pablo Gastaminza and 4 more

Open access · goldAbstract read
In one paragraph

Article in Frontiers in immunology, 2022. 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
2.8field-weighted citation impact, top 8% 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, 28 citations in OpenAlex.

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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

14 authors at 4 institutions in 1 country.

José M CasasnovasDepartments of Macromolecule Structure, Microbial Biotechnology, and Cellular and Molecular Biology, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (CNB-CSIC), Madrid, Spain.
Yago MargollesDepartments of Macromolecule Structure, Microbial Biotechnology, and Cellular and Molecular Biology, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (CNB-CSIC), Madrid, Spain.
María A NoriegaDepartments of Macromolecule Structure, Microbial Biotechnology, and Cellular and Molecular Biology, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (CNB-CSIC), Madrid, Spain.
María GuzmánDepartments of Macromolecule Structure, Microbial Biotechnology, and Cellular and Molecular Biology, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (CNB-CSIC), Madrid, Spain.
Rocío ArranzDepartments of Macromolecule Structure, Microbial Biotechnology, and Cellular and Molecular Biology, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (CNB-CSIC), Madrid, Spain.
Roberto MeleroDepartments of Macromolecule Structure, Microbial Biotechnology, and Cellular and Molecular Biology, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (CNB-CSIC), Madrid, Spain.
Mercedes CasanovaDepartments of Macromolecule Structure, Microbial Biotechnology, and Cellular and Molecular Biology, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (CNB-CSIC), Madrid, Spain.
Juan Alberto CorberaInstituto Universitario de Investigaciones Biomédicas y Sanitarias (IUIBS), Facultad de Veterinaria, Universidad de Las Palmas de Gran Canaria (ULPGC), Campus Universitario de Arucas, Arucas, Spain.
Nereida Jiménez-de-OyaDepartment of Biotechnology, Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria, Consejo Superior de Investigaciones Científicas (INIA, CSIC), Madrid, Spain.
Pablo GastaminzaDepartments of Macromolecule Structure, Microbial Biotechnology, and Cellular and Molecular Biology, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (CNB-CSIC), Madrid, Spain.
Urtzi GaraigortaDepartments of Macromolecule Structure, Microbial Biotechnology, and Cellular and Molecular Biology, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (CNB-CSIC), Madrid, Spain.
Juan Carlos SaizDepartment of Biotechnology, Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria, Consejo Superior de Investigaciones Científicas (INIA, CSIC), Madrid, Spain.
Miguel Ángel Martín-AcebesDepartment of Biotechnology, Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria, Consejo Superior de Investigaciones Científicas (INIA, CSIC), Madrid, Spain.
Luis Ángel FernándezDepartments of Macromolecule Structure, Microbial Biotechnology, and Cellular and Molecular Biology, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (CNB-CSIC), Madrid, Spain.
Centro Nacional de Biotecnología · ESConsejo Superior de Investigaciones Científicas · ESInstituto Nacional de Investigación y Tecnología Agraria y Alimentaria · ESUniversidad de Las Palmas de Gran Canaria · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The emergence of SARS-CoV-2 variants that escape from immune neutralization are challenging vaccines and antibodies developed to stop the COVID-19 pandemic. Thus, it is important to establish therapeutics directed toward multiple or specific SARS-CoV-2 variants. The envelope spike (S) glycoprotein of SARS-CoV-2 is the key target of neutralizing antibodies (Abs). We selected a panel of nine nanobodies (Nbs) from dromedary camels immunized with the receptor-binding domain (RBD) of the S, and engineered Nb fusions as humanized heavy chain Abs (hcAbs). Nbs and derived hcAbs bound with subnanomolar or picomolar affinities to the S and its RBD, and S-binding cross-competition clustered them in two different groups. Most of the hcAbs hindered RBD binding to its human ACE2 (hACE2) receptor, blocked cell entry of viruses pseudotyped with the S protein and neutralized SARS-CoV-2 infection in cell cultures. Four potent neutralizing hcAbs prevented the progression to lethal SARS-CoV-2 infection in hACE2-transgenic mice, demonstrating their therapeutic potential. Cryo-electron microscopy identified Nb binding epitopes in and out the receptor binding motif (RBM), and showed different ways to prevent virus binding to its cell entry receptor. The Nb binding modes were consistent with its recognition of SARS-CoV-2 RBD variants; mono and bispecific hcAbs efficiently bound all variants of concern except omicron, which emphasized the immune escape capacity of this latest variant.

Indexed as

COVID-19Single-Domain AntibodiesAnimalsCryoelectron MicroscopyEpitopesHumansMicePandemicsSARS-CoV-2Spike Glycoprotein, CoronavirusEpitopesSingle-Domain AntibodiesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2coronavirusCOVID-19nanobodiesneutralizing antibodiesSARS-CoV-2 variants

Identifiers

PMID35547740
PMCPMC9082315
OpenAlexW4224444443

What OpenQuestion holds

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Registered trials

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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.