Evidence map›Paper›PMID 31720928›Full record

ArticleMolecular biotechnology2020

A Novel Nanobody Scaffold Optimized for Bacterial Expression and Suitable for the Construction of Ribosome Display Libraries.

Davide Ferrari, Valentina Garrapa, Massimo Locatelli, Angelo Bolchi

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Construction and validation of a synthetic phage-displayed nanobody library.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2024
    Article
  6. Article
  7. Article
  8. NANOBODYInternational journal of molecular sciences · 2023
    Review
  9. Nanobodies: Robust miniprotein binders in biomedicine.Advanced drug delivery reviews · 2023
    Review
  10. Review
  11. Review
  12. Review
  13. Exploring cellular biochemistry with nanobodies.The Journal of biological chemistry · 2020
    Review
  14. Review
  15. Nanobodies-Useful Tools for Allergy Treatment?Frontiers in immunology · 2020
    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

4 authors at 1 institution in 1 country.

Davide FerrariDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, Parco area delle Scienze, 11A, 43124, Parma, Italy. davide.ferrari@unipr.it.ORCID http://orcid.org/0000-0001-7084-6800
Valentina GarrapaDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, Parco area delle Scienze, 11A, 43124, Parma, Italy.
Massimo LocatelliSan Raffaele Hospital, via Olgettina 60, 20132, Milan, Italy.
Angelo BolchiDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, Parco area delle Scienze, 11A, 43124, Parma, Italy.ORCID http://orcid.org/0000-0002-2647-7531
University of Parma · IT

Funding

Regione Emilia-Romagna PRUa1RI-2012-006
6 · The paper itself

Abstract

Single-domain antigen-binding fragments of camelid antibodies, known as VHHs or nanobodies, are widely used affinity reagents. However, their production involving animal immunization is time- and resource-intensive. Starting from a sequence dataset of llama VHHs, we designed a novel scaffold, based on conserved framework sequences, suitable for bacterial nanobody expression and synthetic library construction. The consensus scaffold was validated by grafting the CDRs from two known nanobodies. While maintaining their binding properties, the two chimeric nanobodies showed higher levels of expression and solubility in E. coli when compared to the corresponding wild types. A proof-of-concept synthetic combinatorial library, suitable for ribosome display (RD) selection, was obtained by encoding three randomized complementarity determining regions within the consensus framework. The library, made of linear DNA fragments, has an estimated complexity of > 10

Indexed as

Amino Acid SequenceAnimalsAntibody AffinityCamelusCloning, MolecularDirected Molecular EvolutionEscherichia coliGene ExpressionPeptide LibraryProtein EngineeringRecombinant Fusion ProteinsRibosomesSingle-Domain AntibodiesPeptide LibraryRecombinant Fusion ProteinsSingle-Domain AntibodiesLibraryNanobodyRibosome displayScaffoldVHH

Identifiers

PMID31720928
OpenAlexW2988960315

What OpenQuestion holds

Textmetadata
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.