Evidence map›Paper›PMID 29896285›Full record

ArticleJournal of Cancer2018

Construction of a human monoclonal antibody against bFGF for suppression of NSCLC.

Sheng Wang, Yiyang Qin, Zhongmin Wang, Junjian Xiang, Yu Zhang, Meng Xu, Baiyong Li, Yu Xia, Peng Zhang, Hong Wang

Open access · goldAbstract read
In one paragraph

Article in Journal of Cancer, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.4field-weighted citation impact, top 40% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. 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

10 authors at 1 institution in 1 country.

Sheng WangGuangdong Province Engineering Research Center for antibody drug and immunoassay, College of Life Science and Technology, Jinan University, Guangzhou 510632, Guangdong Province, China.
Yiyang QinGuangdong Province Engineering Research Center for antibody drug and immunoassay, College of Life Science and Technology, Jinan University, Guangzhou 510632, Guangdong Province, China.
Zhongmin WangAkeso Biopharma, Inc., Zhongshan, 528400, Guangdong Province, China.
Junjian XiangGuangdong Province Engineering Research Center for antibody drug and immunoassay, College of Life Science and Technology, Jinan University, Guangzhou 510632, Guangdong Province, China.
Yu ZhangGuangdong Province Engineering Research Center for antibody drug and immunoassay, College of Life Science and Technology, Jinan University, Guangzhou 510632, Guangdong Province, China.
Meng XuDepartment of Oncology, the First Affiliated Hospital of Jinan University, Guangzhou 510632, Guangdong Province, China.
Baiyong LiAkeso Biopharma, Inc., Zhongshan, 528400, Guangdong Province, China.
Yu XiaAkeso Biopharma, Inc., Zhongshan, 528400, Guangdong Province, China.
Peng ZhangAkeso Biopharma, Inc., Zhongshan, 528400, Guangdong Province, China.
Hong WangGuangdong Province Engineering Research Center for antibody drug and immunoassay, College of Life Science and Technology, Jinan University, Guangzhou 510632, Guangdong Province, China.
First Affiliated Hospital of Jinan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Compelling evidence implicates that overexpression of basic fibroblast growth factor (bFGF) and fibroblast growth factor receptor 1 (FGFR1) in non-small cell lung cancer (NSCLC) drives tumor progression, can serve as prognostic biomarkers or therapeutic targets for NSCLC patients. But at present, we still lack of effective drugs for bFGF. The preparation of monoclonal antibodies against bFGF or to understand its mechanism of action is urgently need. Previously, we used hybridoma technology to produce a murine anti-bFGF monoclonal antibody (E12). However, E12 carries risks of heterogeneity and immunogenicity. In the present work, we produced three humanized variants (H1L1, H2L2 and H3L3) based on E12 by substituting residues in or near the complementarity-determining region (CDR). In addition, we thoroughly explored VH/VL domain combinations to simulate full-length IgG1 antibodies using computational protein design. H3L3 was selected for further study, as it demonstrated the best humanization and strongest affinity for bFGF. Specially, humanization of H3L3's light chain and heavy chain were 100% and 98.89%, respectively. The FGF2 neutralizing effect of H3L3 were confirmed by ELISA. We also found that H3L3 can effectively suppress the growth and angiogenesis of cancer through reduce the phosphorylation of AKT and MAPK. Moreover, H3L3 dramatically reduced tumor size and micro-vessel density in nude mice. Altogether, our study demonstrates that H3L3 exerts anti-tumor effects by impeding NSCLC development.

Indexed as

Antibody humanizationbFGFNon-Small Cell LungTargeted therapies

Identifiers

PMID29896285
PMCPMC5995934
OpenAlexW2803937591

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.