Evidence map›Paper›PMID 31359103›Full record

ArticleApplied microbiology and biotechnology2019

In vitro affinity maturation of antibody against membrane-bound GPCR molecules.

Jie Wang, Lili An, Yun Zhao, Cheng Zhang, Shengnan Li, Chen Ye, Shuqian Jing, Haiying Hang

Open access · hybridAbstract read
In one paragraph

Article in Applied microbiology and biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

7 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Deep learning guided optimization of human antibody against SARS-CoV-2 variants with broad neutralization.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Progress toward improved understanding of antibody maturation.Current opinion in structural biology · 2021
    Review
  7. 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 3 institutions in 1 country.

Jie WangKey Laboratory for Protein and Peptide Pharmaceuticals, National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Lili AnKey Laboratory for Protein and Peptide Pharmaceuticals, National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Yun ZhaoKey Laboratory for Protein and Peptide Pharmaceuticals, National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Cheng ZhangGmax Biopharm LLC, Hangzhou, 310052, China.
Shengnan LiGmax Biopharm LLC, Hangzhou, 310052, China.
Chen YeKey Laboratory for Protein and Peptide Pharmaceuticals, National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Shuqian JingGmax Biopharm LLC, Hangzhou, 310052, China. sjing@gmaxbiopharm.com.
Haiying HangKey Laboratory for Protein and Peptide Pharmaceuticals, National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China. hh91@ibp.ac.cn.
Chinese Academy of Sciences · CNUniversity of Chinese Academy of Sciences · CNInstitute of Biophysics · CN

Funding

Beijing Science and Technology Project Z181100003818023Development of Ministry of Science and Technology 2014CB910402National Key R&D Program of China 2017YFF0205404National Natural Science Foundation of China No. 31870923
6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs), also known as seven-transmembrane domain receptors, are among the most important targets against which many small molecule drugs have been developed. However, only two antibody drugs targeting GPCRs have been approved for clinical use although many antibody drugs against non-GPCR protein targets have been successfully developed for various disease indications. One of the challenges for developing anti-GPCR drugs is the high difficulty to perform affinity maturation due to their insolubility in aqueous solutions. To address this issue, CHO cell display libraries of single-chain variable fragments (scFvs) and full-length antibodies were maturated directly against vesicle probes prepared from CHO cells displaying the endothelin A receptor (ETaR) GPCR. The probe in the vesicle form ensures the physiological conformation and functional activity of the protein and avoids issues with membrane protein insolubility. The size of the vesicle had a clear effect on protein-ligand interaction; we used small-sized vesicles with low expression levels of GPCRs for the affinity maturation. Four rounds of affinity maturation combining vesicles as probes with the CHO cell display platform improved affinity by 13.58-fold for scFvs and 5.05-fold for full-length antibodies. We expect that this method will not only be used for the affinity maturation of antibodies against GPCRs but will also be used to mature antibodies for other types of proteins where the conformation/activity of which depends on the proper membrane environment.

Indexed as

Antibody AffinityAnimalsCHO CellsCricetulusLigandsMolecular ConformationReceptor, Endothelin ASingle-Chain AntibodiesLigandsReceptor, Endothelin ASingle-Chain AntibodiesAffinity maturationCHO cell displayETaRGPCRVesicle

Identifiers

PMID31359103
PMCPMC6719327
OpenAlexW2965717316

What Socratic 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 Socratic graph.