Evidence map›Paper›PMID 31544875›Full record

ArticleAntibodies (Basel, Switzerland)2018

OptMAVEn-2.0: De novo Design of Variable Antibody Regions against Targeted Antigen Epitopes.

Ratul Chowdhury, Matthew F Allan, Costas D Maranas

Open access · goldAbstract read
In one paragraph

Article in Antibodies (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

27 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Article
  3. Antibody Affinity Maturation by Computational Design.Methods in molecular biology (Clifton, N.J.) · 2026
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  4. Review
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  14. How can we discover developable antibody-based biotherapeutics?Frontiers in molecular biosciences · 2023
    Review
  15. Article
  16. Article
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  18. Article
  19. IsAb: a computational protocol for antibody design.Briefings in bioinformatics · 2021
    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

3 authors at 1 institution in 1 country.

Ratul ChowdhuryDepartment of Chemical Engineering, The Pennsylvania State University, State College, PA 16802, USA. ratul@psu.edu.ORCID 0000-0003-4522-6911
Matthew F AllanDepartment of Chemical Engineering, The Pennsylvania State University, State College, PA 16802, USA. mfallan@mit.edu.
Costas D MaranasDepartment of Chemical Engineering, The Pennsylvania State University, State College, PA 16802, USA. costas@psu.edu.
Pennsylvania State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Monoclonal antibodies are becoming increasingly important therapeutic agents for the treatment of cancers, infectious diseases, and autoimmune disorders. However, laboratory-based methods of developing therapeutic monoclonal antibodies (e.g., immunized mice, hybridomas, and phage display) are time-consuming and are often unable to target a specific antigen epitope or reach (sub)nanomolar levels of affinity. To this end, we developed Optimal Method for Antibody Variable region Engineering (OptMAVEn) for de novo design of humanized monoclonal antibody variable regions targeting a specific antigen epitope. In this work, we introduce OptMAVEn-2.0, which improves upon OptMAVEn by (1) reducing computational resource requirements without compromising design quality; (2) clustering the designs to better identify high-affinity antibodies; and (3) eliminating intra-antibody steric clashes using an updated set of clashing parts from the Modular Antibody Parts (MAPs) database. Benchmarking on a set of 10 antigens revealed that OptMAVEn-2.0 uses an average of 74% less CPU time and 84% less disk storage relative to OptMAVEn. Testing on 54 additional antigens revealed that computational resource requirements of OptMAVEn-2.0 scale only sub-linearly with respect to antigen size. OptMAVEn-2.0 was used to design and rank variable antibody fragments targeting five epitopes of Zika envelope protein and three of hen egg white lysozyme. Among the top five ranked designs for each epitope, recovery of native residue identities is typically 45-65%. MD simulations of two designs targeting Zika suggest that at least one would bind with high affinity. OptMAVEn-2.0 can be downloaded from our GitHub repository and webpage as (links in Summary and Discussion section).

Indexed as

computational protein designde novo antibody designspecific antigen epitopezika envelope protein

Identifiers

PMID31544875
PMCPMC6640672
OpenAlexW2811051657

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.