Evidence map›Paper›PMID 28486528›Full record

ArticlePloS one2017

Identification and characterization of a neutralizing monoclonal antibody that provides complete protection against Yersinia pestis.

Weicen Liu, Jun Ren, Jinlong Zhang, Xiaohong Song, Shuling Liu, Xiangyang Chi, Yi Chen, Zhonghua Wen, Jianmin Li, Wei Chen

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. 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
1.1field-weighted citation impact, top 19% 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, 11 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Vaccines · 2020
    Article
  9. Development of Anti-ImmunoTargets and therapy · 2020
    Article
  10. 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.

Weicen LiuLaboratory of Vaccine and Antibody Engineering, Beijing Institute of Biotechnology, 20 FengTai Dongdajie Street, Beijing, PR China.ORCID http://orcid.org/0000-0001-6235-5251
Jun RenLaboratory of Vaccine and Antibody Engineering, Beijing Institute of Biotechnology, 20 FengTai Dongdajie Street, Beijing, PR China.
Jinlong ZhangLaboratory of Vaccine and Antibody Engineering, Beijing Institute of Biotechnology, 20 FengTai Dongdajie Street, Beijing, PR China.
Xiaohong SongLaboratory of Vaccine and Antibody Engineering, Beijing Institute of Biotechnology, 20 FengTai Dongdajie Street, Beijing, PR China.
Shuling LiuLaboratory of Vaccine and Antibody Engineering, Beijing Institute of Biotechnology, 20 FengTai Dongdajie Street, Beijing, PR China.
Xiangyang ChiLaboratory of Vaccine and Antibody Engineering, Beijing Institute of Biotechnology, 20 FengTai Dongdajie Street, Beijing, PR China.
Yi ChenLaboratory of Vaccine and Antibody Engineering, Beijing Institute of Biotechnology, 20 FengTai Dongdajie Street, Beijing, PR China.
Zhonghua WenLaboratory of Vaccine and Antibody Engineering, Beijing Institute of Biotechnology, 20 FengTai Dongdajie Street, Beijing, PR China.
Jianmin LiLaboratory of Vaccine and Antibody Engineering, Beijing Institute of Biotechnology, 20 FengTai Dongdajie Street, Beijing, PR China.
Wei ChenLaboratory of Vaccine and Antibody Engineering, Beijing Institute of Biotechnology, 20 FengTai Dongdajie Street, Beijing, PR China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Yersinia pestis (Y. pestis) has caused an alarming number of deaths throughout recorded human history, and novel prophylactics and therapeutics are necessary given its potential as a bioweapon. Only one monoclonal antibody has been identified to date that provides complete protection against Y. pestis. Here, we describe a second novel murine monoclonal antibody (F2H5) that provided complete protection against Y. pestis 141 infection when administered prophylactically to Balb/c mice (100 μg intravenously). We humanized F2H5, characterized its ability to bind to the Y. pestis F1 protein and further characterized the neutralizing epitope using computational and experimental approaches. While Western blot results suggested a linear epitope, peptide mapping using ELISA failed to identify an epitope, suggesting a conformational epitope instead. We adopted a computational approach based on Residue Contact Frequency to predict the site of antigen-antibody interaction and defined the F2H5/F1 binding site computationally. Based on computational approach, we determined that residues G104E105N106 in F1 were critical to F2H5 binding and that CDRH2 and CDRH3 of F2H5 interacted with F1. Our results show that combining computational approach and experimental approach can effectively identify epitopes.

Indexed as

Antibodies, MonoclonalAntibodies, NeutralizingHumansYersinia pestisAntibodies, MonoclonalAntibodies, Neutralizing

Identifiers

PMID28486528
PMCPMC5423616
OpenAlexW2612954538

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.