Evidence map›Paper›PMID 23384000›Full record

ArticleJournal of computational biology : a journal of computational molecular cell biology2013

Structure-guided deimmunization of therapeutic proteins.

Andrew S Parker, Yoonjoo Choi, Karl E Griswold, Chris Bailey-Kellogg

Abstract read
In one paragraph

Article in Journal of computational biology : a journal of computational molecular cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
9.3field-weighted citation impact, top 1% 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

41 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
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  3. Review
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  6. Optimizing Antibody-Antigen Binding Affinities with the ADAPT Platform.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Protein Design by Provable Algorithms.Communications of the ACM · 2019
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Computationally optimized deimmunization libraries yield highly mutated enzymes with low immunogenicity and enhanced activity.Proceedings of the National Academy of Sciences of the United States of America · 2017
    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

4 authors at 1 institution in 1 country.

Andrew S ParkerDepartment of Computer Science, Dartmouth College, Hanover, NH 03755, USA.
Yoonjoo Choi
Karl E Griswold
Chris Bailey-Kellogg
Dartmouth College · US

Funding

Functional Deimmunization of Therapeutic ProteinsR01GM098977 · NIGMS · DARTMOUTH COLLEGE · PI BAILEY-KELLOGG, CHRIS, GRISWOLD, KARL E · 2011 to 2019
$3.4M
NIGMS NIH HHS R01 GM098977NIGMS NIH HHS R01-GM-098977
6 · The paper itself

Abstract

Therapeutic proteins continue to yield revolutionary new treatments for a growing spectrum of human disease, but the development of these powerful drugs requires solving a unique set of challenges. For instance, it is increasingly apparent that mitigating potential anti-therapeutic immune responses, driven by molecular recognition of a therapeutic protein's peptide fragments, may be best accomplished early in the drug development process. One may eliminate immunogenic peptide fragments by mutating the cognate amino acid sequences, but deimmunizing mutations are constrained by the need for a folded, stable, and functional protein structure. These two concerns may be competing, as the mutations that are best at reducing immunogenicity often involve amino acids that are substantially different physicochemically. We develop a novel approach, called EpiSweep, that simultaneously optimizes both concerns. Our algorithm identifies sets of mutations making such Pareto optimal trade-offs between structure and immunogenicity, embodied by a molecular mechanics energy function and a T-cell epitope predictor, respectively. EpiSweep integrates structure-based protein design, sequence-based protein deimmunization, and algorithms for finding the Pareto frontier of a design space. While structure-based protein design is NP-hard, we employ integer programming techniques that are efficient in practice. Furthermore, EpiSweep only invokes the optimizer once per identified Pareto optimal design. We show that EpiSweep designs of regions of the therapeutics erythropoietin and staphylokinase are predicted to outperform previous experimental efforts. We also demonstrate EpiSweep's capacity for deimmunization of the entire proteins, case analyses involving dozens of predicted epitopes, and tens of thousands of unique side-chain interactions. Ultimately, Epi-Sweep is a powerful protein design tool that guides the protein engineer toward the most promising immunotolerant biotherapeutic candidates.

Indexed as

AlgorithmsAmino Acid MotifsAmino AcidsAntigenic VariationBacterial ProteinsComputer-Aided DesignDrug DesignEpitopes, T-LymphocyteErythropoietinHumansMetalloendopeptidasesModels, MolecularMolecular Sequence DataProtein BindingProtein EngineeringThermodynamicsAmino AcidsauR protein, Staphylococcus aureusBacterial ProteinsEpitopes, T-LymphocyteErythropoietinMetalloendopeptidases

Identifiers

PMID23384000
PMCPMC3576912
OpenAlexW2389336060

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.