Evidence map›Paper›PMID 35030983›Full record

ArticlemAbs

Computational design of a neutralizing antibody with picomolar binding affinity for all concerning SARS-CoV-2 variants.

Bo-Seong Jeong, Jeong Seok Cha, Insu Hwang, Uijin Kim, Jared Adolf-Bryfogle, Brian Coventry, Hyun-Soo Cho, Kyun-Do Kim, Byung-Ha Oh

Abstract 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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Article
  2. Discovery of TCR-like antibodies to the KRAS G12D neoantigen via in silico-in vitro workflow.Molecular therapy : the journal of the American Society of Gene Therapy · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
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

9 authors.

Bo-Seong JeongDepartment of Biological Sciences, Kaist Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon, Republic of Korea.ORCID 0000-0003-0629-6722
Jeong Seok ChaDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul, Republic of Korea.
Insu HwangCenter for Convergent Research of Emerging Virus Infection, Korea Research Institute of Chemical Technology, Daejeon, Republic of Korea.
Uijin KimDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul, Republic of Korea.
Jared Adolf-BryfogleInstitute for Protein Innovation, Boston, MA, USA.
Brian CoventryMolecular Engineering & Sciences Institute & Institute for Protein Design, University of Washington, Seattle, Washington, USA.
Hyun-Soo ChoDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul, Republic of Korea.
Kyun-Do KimCenter for Convergent Research of Emerging Virus Infection, Korea Research Institute of Chemical Technology, Daejeon, Republic of Korea.
Byung-Ha OhDepartment of Biological Sciences, Kaist Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon, Republic of Korea.ORCID 0000-0002-6437-8470

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Coronavirus disease 2019, caused by SARS-CoV-2, remains an on-going pandemic, partly due to the emergence of variant viruses that can "break-through" the protection of the current vaccines and neutralizing antibodies (nAbs), highlighting the needs for broadly nAbs and next-generation vaccines. We report an antibody that exhibits breadth and potency in binding the receptor-binding domain (RBD) of the virus spike glycoprotein across SARS coronaviruses. Initially, a lead antibody was computationally discovered and crystallographically validated that binds to a highly conserved surface of the RBD of wild-type SARS-CoV-2. Subsequently, through experimental affinity enhancement and computational affinity maturation, it was further developed to bind the RBD of all concerning SARS-CoV-2 variants, SARS-CoV-1 and pangolin coronavirus with pico-molar binding affinities, consistently exhibited strong neutralization activity against wild-type SARS-CoV-2 and the Alpha and Delta variants. These results identify a vulnerable target site on coronaviruses for development of pan-sarbecovirus nAbs and vaccines.

Indexed as

Angiotensin-Converting Enzyme 2Antibodies, ViralAntibody AffinityAntibody SpecificityAntigen-Antibody ReactionsAntigens, ViralBroadly Neutralizing AntibodiesCOVID-19Crystallography, X-RayEpitopesHumansImmunoglobulin FragmentsMolecular Docking SimulationMonte Carlo MethodNeutralization TestsPeptide FragmentsACE2 protein, humanAngiotensin-Converting Enzyme 2Antibodies, ViralAntigens, ViralBroadly Neutralizing AntibodiesEpitopesImmunoglobulin Fragmentsimmunoglobulin FvPeptide FragmentsRecombinant Fusion ProteinsSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2broadly neutralizing antibodybroad-spectrum vaccineComputational antibody discoveryemerging variantsSars-CoV-2

Identifiers

PMID35030983
PMCPMC8765073

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.