Evidence map›Paper›PMID 37990030›Full record

ArticleScientific reports2023

High-throughput analysis system of interaction kinetics for data-driven antibody design.

Ryo Matsunaga, Kan Ujiie, Mayuko Inagaki, Jorge Fernández Pérez, Yoshiki Yasuda, Shinya Mimasu, Shinji Soga, Kouhei Tsumoto

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

10 citing papers in PubMed, 15 citations in OpenAlex.

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  10. High-throughput system for the thermostability analysis of proteins.Protein science : a publication of the Protein Society · 2024
    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

8 authors at 2 institutions in 1 country.

Ryo MatsunagaDepartment of Bioengineering, School of Engineering, The University of Tokyo, Tokyo, 113-8656, Japan.
Kan UjiieDepartment of Bioengineering, School of Engineering, The University of Tokyo, Tokyo, 113-8656, Japan.
Mayuko InagakiDepartment of Bioengineering, School of Engineering, The University of Tokyo, Tokyo, 113-8656, Japan.
Jorge Fernández PérezDepartment of Bioengineering, School of Engineering, The University of Tokyo, Tokyo, 113-8656, Japan.
Yoshiki YasudaDepartment of Chemistry and Biotechnology, School of Engineering, The University of Tokyo, Tokyo, 113-8656, Japan.
Shinya MimasuBiologics Engineering, Discovery Intelligence, Astellas Pharma Inc., 21, Miyukigaoka, Tsukuba-shi, Ibaraki, 305-8585, Japan.
Shinji SogaBiologics Engineering, Discovery Intelligence, Astellas Pharma Inc., 21, Miyukigaoka, Tsukuba-shi, Ibaraki, 305-8585, Japan.
Kouhei TsumotoDepartment of Bioengineering, School of Engineering, The University of Tokyo, Tokyo, 113-8656, Japan. tsumoto@bioeng.t.u-tokyo.ac.jp.
The University of Tokyo · JPAstellas Pharma (Japan) · JP

Funding

JST ACT-X JPMJAX222IJST CREST JPMJCR20H8MEXT Data Creation and Utilization-Type Material Research and Development Project JPMXP1122714694
6 · The paper itself

Abstract

Surface plasmon resonance (SPR) is widely used for antigen-antibody interaction kinetics analysis. However, it has not been used in the screening phase because of the low throughput of measurement and analysis. Herein, we proposed a high-throughput SPR analysis system named "BreviA" using the Brevibacillus expression system. Brevibacillus was transformed using a plasmid library containing various antibody sequences, and single colonies were cultured in 96-well plates. Sequence analysis was performed using bacterial cells, and recombinant antibodies secreted in the supernatant were immobilized on a sensor chip to analyze their interactions with antigens using high-throughput SPR. Using this system, the process from the transformation to 384 interaction analyses can be performed within a week. This system utility was tested using an interspecies specificity design of an anti-human programmed cell death protein 1 (PD-1) antibody. A plasmid library containing alanine and tyrosine mutants of all complementarity-determining region residues was generated. A high-throughput SPR analysis was performed against human and mouse PD-1, showing that the mutation in the specific region enhanced the affinity for mouse PD-1. Furthermore, deep mutational scanning of the region revealed two mutants with > 100-fold increased affinity for mouse PD-1, demonstrating the potential efficacy of antibody design using data-driven approach.

Indexed as

AntibodiesProgrammed Cell Death 1 ReceptorAnimalsAntigensComplementarity Determining RegionsHumansKineticsMiceSurface Plasmon ResonanceAntibodiesAntigensComplementarity Determining RegionsProgrammed Cell Death 1 Receptor

Identifiers

PMID37990030
PMCPMC10663500
OpenAlexW4388865160

What OpenQuestion holds

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LicenceCC BY
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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.