Evidence map›Paper›PMID 19679153›Full record

ReviewAdvanced drug delivery reviews2009

Removal of B cell epitopes as a practical approach for reducing the immunogenicity of foreign protein-based therapeutics.

Satoshi Nagata, Ira Pastan

Open access · greenAbstract readReview
In one paragraph

Review in Advanced drug delivery reviews, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

49 citing papers in PubMed, 79 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Synthesis of an Anti-CD7 Recombinant Immunotoxin Based on PE24 in CHO andInternational journal of molecular sciences · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Systems Biology Approaches for Therapeutics Development Against COVID-19.Frontiers in cellular and infection microbiology · 2020
    Review
  18. Immunogenicity of Immunotoxins ContainingFrontiers in immunology · 2020
    Review
  19. Article
  20. 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

2 authors at 2 institutions in 1 country.

Satoshi NagataCancer Biology Research Center, Sanford Research/USD, Sioux Falls, SD 57105, USA. nagatas@sanfordhealth.org
Ira Pastan
National Cancer Institute · USSanford Research · US

Funding

Immunotoxin Therapy of Solid and Hematopoietic Tumors: Preclinical StudiesZIABC008753 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI PASTAN, IRA · 2009 to 2024
$33.1M
IMMUNOTOXIN THERAPY OF SOLID AND HEMATOPOIETIC TUMORS: PRECLINICAL STUDIESZ01BC008753 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI PASTAN, IRA · 1996 to 2008
$3.2M
Intramural NIH HHS Z01 BC008753
6 · The paper itself

Abstract

Immunogenicity of non-human proteins with useful therapeutic properties has prevented their development for use in the therapy of disease. However, this class of proteins could be very useful, if their immunogenicity could be markedly reduced so that many treatment cycles could be administered. One approach to reduce the immunogenicity of foreign proteins is to identify B cell epitopes on the protein and eliminate them by mutagenesis. In this article, theoretical aspects and experimental evidence for the feasibility of B cell epitope removal is reviewed. A special focus is given to our results with deimmunization of recombinant immunotoxins in which Fvs are fused to a 38kDa portion of the bacterial protein, Pseudomonas exotoxin A (PE38). Immunotoxins targeting CD22 and CD25 have produced complete remissions in many patients with drug resistant Hairy Cell Leukemia and are being evaluated in other malignancies. Experimental data summarized in this review indicates that removal of B cell epitopes is a practical approach for making less immunogenic protein therapeutics from non-human functional proteins. This approach requires grouping of the epitopes to identify targets for deimmunization followed by quantitative analysis of the decrease in affinity produced by the mutations in B cell epitopes.

Indexed as

Epitopes, B-LymphocyteAnimalsAntibody AffinityAntigen-Antibody ReactionsEpitopes, T-LymphocyteHumansImmunotoxinsMutagenesisPoint MutationProtein ConformationProteinsEpitopes, B-LymphocyteEpitopes, T-LymphocyteImmunotoxinsProteins

Identifiers

PMID19679153
PMCPMC2757538
OpenAlexW1992650953

What OpenQuestion holds

Textmetadata
LicenceTDM
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.