Evidence map›Paper›PMID 33322557›Full record

ArticleBiomolecules2020

Picomolar SARS-CoV-2 Neutralization Using Multi-Arm PEG Nanobody Constructs.

Ainhoa Moliner-Morro, Daniel J Sheward, Vivien Karl, Laura Perez Vidakovics, Ben Murrell, Gerald M McInerney, Leo Hanke

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed, 1 pooled it
3.1field-weighted citation impact, top 6% 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

31 citing papers in PubMed, 1 synthesis or guideline pooled it, 45 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Amino acid variants at the P94 position inbioRxiv : the preprint server for biology · 2026
    Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. A Novel Anti-CD47 Nanobody Tetramer for Cancer Therapy.Antibodies (Basel, Switzerland) · 2024
    Article
  16. Review
  17. NANOBODYInternational journal of molecular sciences · 2023
    Review
  18. Review
  19. Article
  20. Review
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

7 authors at 2 institutions in 2 countries.

Ainhoa Moliner-MorroDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, 17177 Stockholm, Sweden.ORCID 0000-0001-8963-3063
Daniel J ShewardDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, 17177 Stockholm, Sweden.
Vivien KarlDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, 17177 Stockholm, Sweden.
Laura Perez VidakovicsDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, 17177 Stockholm, Sweden.ORCID 0000-0003-4283-812X
Ben MurrellDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, 17177 Stockholm, Sweden.
Gerald M McInerneyDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, 17177 Stockholm, Sweden.ORCID 0000-0003-2257-7241
Leo HankeDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, 17177 Stockholm, Sweden.ORCID 0000-0001-5514-2418
Karolinska Institutet · SEUniversity of Cape Town · ZA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Multivalent antibody constructs have a broad range of clinical and biotechnological applications. Nanobodies are especially useful as components for multivalent constructs as they allow increased valency while maintaining a small molecule size. We here describe a novel, rapid method for the generation of bi- and multivalent nanobody constructs with oriented assembly by Cu-free strain promoted azide-alkyne click chemistry (SPAAC). We used sortase A for ligation of click chemistry functional groups site-specifically to the C-terminus of nanobodies before creating C-to-C-terminal nanobody fusions and 4-arm polyethylene glycol (PEG) tetrameric nanobody constructs. We demonstrated the viability of this approach by generating constructs with the SARS-CoV-2 neutralizing nanobody Ty1. We compared the ability of the different constructs to neutralize SARS-CoV-2 pseudotyped virus and infectious virus in neutralization assays. The generated dimers neutralized the virus similarly to a nanobody-Fc fusion variant, while a 4-arm PEG based tetrameric Ty1 construct dramatically enhanced neutralization of SARS-CoV-2, with an IC

Indexed as

Antibodies, NeutralizingClick ChemistryCOVID-19COVID-19 Drug TreatmentHumansSARS-CoV-2Single-Domain AntibodiesAntibodies, NeutralizingSingle-Domain Antibodiesclick chemistrymultivalentnanobodyneutralizationPEG linkerSARS-CoV-2Single-domain antibody fragmentsortase A

Identifiers

PMID33322557
PMCPMC7764822
OpenAlexW3112906777

What OpenQuestion 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 OpenQuestion graph.