Evidence map›Paper›PMID 28605292›Full record

ArticleHuman vaccines & immunotherapeutics2017

Targeting the gram-negative bacteria peptidoglycan synthase MraY as a new approach for monoclonal antibody anti-bacterial activity.

Jun Cao, Fei Yi, Qiufeng Tian, Guanghui Dang, Wei Si, Siguo Liu, Shenye Yu

Open access · bronzeAbstract read
In one paragraph

Article in Human vaccines & immunotherapeutics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 27% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Monoclonal antibody-based therapies for bacterial infections.Current opinion in infectious diseases · 2019
    Review
  6. 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

7 authors at 2 institutions in 1 country.

Jun Caoa Division of Bacterial Diseases, State Key Laboratory of Veterinary Biotechnology , Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences , Harbin , PR China.
Fei Yia Division of Bacterial Diseases, State Key Laboratory of Veterinary Biotechnology , Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences , Harbin , PR China.
Qiufeng Tiana Division of Bacterial Diseases, State Key Laboratory of Veterinary Biotechnology , Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences , Harbin , PR China.
Guanghui Danga Division of Bacterial Diseases, State Key Laboratory of Veterinary Biotechnology , Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences , Harbin , PR China.
Wei Sia Division of Bacterial Diseases, State Key Laboratory of Veterinary Biotechnology , Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences , Harbin , PR China.
Siguo Liua Division of Bacterial Diseases, State Key Laboratory of Veterinary Biotechnology , Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences , Harbin , PR China.
Shenye Yua Division of Bacterial Diseases, State Key Laboratory of Veterinary Biotechnology , Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences , Harbin , PR China.
Harbin Veterinary Research Institute · CNChinese Academy of Agricultural Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The use of antibiotics to target bacteria is a well-validated approach for controlling infections in animals and humans. Peptidoglycan biosynthesis is a crucial process in bacteria, and the conserved peptidoglycan synthase MraY is an attractive target for drug design. However, due to the lack of detailed MraY structural information, antibiotics targeting MraY have not yet been developed. In the present study, 2 hydrophilic regions of MraY from Escherichia coli were expressed as a fusion protein and used to raise a monoclonal antibody in mice. We confirmed that the MraY amino acid sequence PESHFSKRGTPT forms the core epitope recognized by the monoclonal antibody M-H11. Furthermore, our results show that M-H11 effectively controls Escherichia coli BL21 (DE3) plysS infection, both in vitro and in vivo. Our results may be of great value in the search for novel approaches used to control bacterial infections.

Indexed as

Amino Acid SequenceAnimalsAntibodies, BacterialAntibodies, MonoclonalBacterial ProteinsEpitopesEscherichia coliEscherichia coli InfectionsMicePeptidoglycanTransferasesTransferases (Other Substituted Phosphate Groups)Antibodies, BacterialAntibodies, MonoclonalBacterial ProteinsEpitopesmraY protein, BacteriaPeptidoglycanTransferasesTransferases (Other Substituted Phosphate Groups)anti-bacterial activitymonoclonal antibodytransferase MraY

Identifiers

PMID28605292
PMCPMC5612219
OpenAlexW2624790502

What OpenQuestion holds

Textmetadata
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.