Evidence map›Paper›PMID 27224530›Full record

ArticlemAbs

Discovery of high affinity anti-ricin antibodies by B cell receptor sequencing and by yeast display of combinatorial VH:VL libraries from immunized animals.

Bo Wang, Chang-Han Lee, Erik L Johnson, Christien A Kluwe, Josephine C Cunningham, Hidetaka Tanno, Richard M Crooks, George Georgiou, Andrew D Ellington

Abstract read
PubMed Full text at PMC Publisher
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 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. Article
  2. Review
  3. Article
  4. How repertoire data are changing antibody science.The Journal of biological chemistry · 2020
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Analyzing Immunoglobulin Repertoires.Frontiers in immunology · 2018
    Review
  14. Article
  15. Review
  16. Deep sequencing methods for protein engineering and design.Current opinion in structural biology · 2017
    Review
  17. Article
  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

9 authors.

Bo Wanga Department of Chemical Engineering , University of Texas at Austin , Austin , TX , USA.
Chang-Han Leea Department of Chemical Engineering , University of Texas at Austin , Austin , TX , USA.
Erik L Johnsona Department of Chemical Engineering , University of Texas at Austin , Austin , TX , USA.
Christien A Kluweb Department of Molecular Biosciences , University of Texas at Austin , Austin , TX , USA.
Josephine C Cunninghamb Department of Molecular Biosciences , University of Texas at Austin , Austin , TX , USA.
Hidetaka Tannoa Department of Chemical Engineering , University of Texas at Austin , Austin , TX , USA.
Richard M Crooksb Department of Molecular Biosciences , University of Texas at Austin , Austin , TX , USA.
George Georgioua Department of Chemical Engineering , University of Texas at Austin , Austin , TX , USA.
Andrew D Ellingtonb Department of Molecular Biosciences , University of Texas at Austin , Austin , TX , USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ricin is a toxin that could potentially be used as a bioweapon. We identified anti-ricin A chain antibodies by sequencing the antibody repertoire from immunized mice and by selecting high affinity antibodies using yeast surface display. These methods led to the isolation of multiple antibodies with high (sub-nanomolar) affinity. Interestingly, the antibodies identified by the 2 independent approaches are from the same clonal lineages, indicating for the first time that yeast surface display can identify native antibodies. The new antibodies represent well-characterized reagents for biodefense diagnostics and therapeutics development.

Indexed as

Cell Surface Display TechniquesPeptide LibraryAnimalsAntibodiesAntibody AffinityB-LymphocytesBone Marrow CellsFemaleHigh-Throughput Nucleotide SequencingHumansImmunizationLymph NodesMiceMice, Inbred BALB CReceptors, Antigen, B-CellRicinAntibodiesPeptide LibraryReceptors, Antigen, B-CellRicinRNA, MessengerSingle-Domain AntibodiesAntibody repertoire analysisnext-generation sequencingricin A chainyeast surface display

Identifiers

PMID27224530
PMCPMC4968101

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.