Evidence map›Paper›PMID 35224467›Full record

ArticleiScience2022

A potent alpaca-derived nanobody that neutralizes SARS-CoV-2 variants.

Jules B Weinstein, Timothy A Bates, Hans C Leier, Savannah K McBride, Eric Barklis, Fikadu G Tafesse

Abstract read
In one paragraph

Article in iScience, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Nanobodies targeting SARS-CoV-2 variants.Acta pharmaceutica Sinica. B · 2026
    Review
  2. Review
  3. Mapping SARS-CoV-2 Nucleocapsid Function with Nanobodies.bioRxiv : the preprint server for biology · 2026
    Article
  4. Review
  5. Improving the solubility of single domain antibodies using VH-like hallmark residues.Protein science : a publication of the Protein Society · 2025
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. VInternational journal of molecular sciences · 2022
    Review
  18. 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

6 authors.

Jules B WeinsteinDepartment of Molecular Microbiology and Immunology, Oregon Health and Sciences University, 3181 SW Sam Jackson Park Road, Portland, OR 97239-3098, USA.
Timothy A BatesDepartment of Molecular Microbiology and Immunology, Oregon Health and Sciences University, 3181 SW Sam Jackson Park Road, Portland, OR 97239-3098, USA.
Hans C LeierDepartment of Molecular Microbiology and Immunology, Oregon Health and Sciences University, 3181 SW Sam Jackson Park Road, Portland, OR 97239-3098, USA.
Savannah K McBrideDepartment of Molecular Microbiology and Immunology, Oregon Health and Sciences University, 3181 SW Sam Jackson Park Road, Portland, OR 97239-3098, USA.
Eric BarklisDepartment of Molecular Microbiology and Immunology, Oregon Health and Sciences University, 3181 SW Sam Jackson Park Road, Portland, OR 97239-3098, USA.
Fikadu G TafesseDepartment of Molecular Microbiology and Immunology, Oregon Health and Sciences University, 3181 SW Sam Jackson Park Road, Portland, OR 97239-3098, USA.

Funding

Multidisciplinary Research Training in Pulmonary MedicineT32HL083808 · NHLBI · OREGON HEALTH & SCIENCE UNIVERSITY · PI LEWINSOHN, DAVID M., SLATORE, CHRISTOPHER G. · 2008 to 2025
$5.3M
HIV-1 Gag Precursor Protein InteractionsR01AI152579 · NIAID · OREGON HEALTH & SCIENCE UNIVERSITY · PI BARKLIS, ERIC W · 2020 to 2024
$2.5M
Determining the role of sphingolipids in Mycobacterium tuberculosis infectionR01AI141549 · NIAID · OREGON HEALTH & SCIENCE UNIVERSITY · PI TAFESSE, FIKADU G. · 2020 to 2025
$2.4M
Octet Red384S10OD023413 · OD · OREGON HEALTH & SCIENCE UNIVERSITY · PI BARR-GILLESPIE, PETER GORDON · 2017 to 2017
$318k
NHLBI NIH HHS T32 HL083808NIAID NIH HHS R01 AI141549NIAID NIH HHS R01 AI152579NIH HHS S10 OD023413
6 · The paper itself

Abstract

The spike glycoprotein of SARS-CoV-2 engages with human ACE 2 to facilitate infection. Here, we describe an alpaca-derived heavy chain antibody fragment (VHH), saRBD-1, that disrupts this interaction by competitively binding to the spike protein receptor-binding domain. We further generated an engineered bivalent nanobody construct engineered by a flexible linker and a dimeric Fc conjugated nanobody construct. Both multivalent nanobodies blocked infection at picomolar concentrations and demonstrated no loss of potency against emerging variants of concern including Alpha (B.1.1.7), Beta (B.1.351), Gamma (P.1), Epsilon (B.1.427/429), and Delta (B.1.617.2). saRBD-1 tolerates elevated temperature, freeze-drying, and nebulization, making it an excellent candidate for further development into a therapeutic approach for COVID-19.

Indexed as

Applied microbiologyBioengineeringNanotechnology

Identifiers

PMID35224467
PMCPMC8863326

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.