Evidence map›Paper›PMID 37789311›Full record

ArticleBMC veterinary research2023

Screening of antigenic epitopes related to the adhesion of the avian Escherichia coli Type 1 Fimbrial Agglutinin Domain.

Junhong Chen, Wei Dai, Shengling Cui, Weiqiang Lei, Dingzhen Dai

Open access · goldAbstract read
In one paragraph

Article in BMC veterinary research, 2023. 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
1.5field-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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Avian PathogenicVeterinary sciences · 2025
    Review
  2. Article
  3. Targeting breast cancer: the promise of phage-based nanomedicines.Breast cancer research and treatment · 2025
    Review
  4. 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

5 authors at 2 institutions in 1 country.

Junhong ChenSchool of Animal Science and Food Engineering, Jinling Institute of Technology, Nanjing, 210038, China.
Wei DaiSchool of Animal Science and Food Engineering, Jinling Institute of Technology, Nanjing, 210038, China.
Shengling CuiCollege of Veterinary Medicine, Yangzhou University, Yangzhou, 225009, China.
Weiqiang LeiSchool of Animal Science and Food Engineering, Jinling Institute of Technology, Nanjing, 210038, China.
Dingzhen DaiSchool of Animal Science and Food Engineering, Jinling Institute of Technology, Nanjing, 210038, China. dzdai@163.com.
Jinling Institute of Technology · CNYangzhou University · CN

Funding

The Natural Science Foundation of Jiangsu Province BK20210005The Natural Science Foundation of the Jiangsu Higher Education Institutions of China 19KJB230006
6 · The paper itself

Abstract

backgroundAvian Escherichia coli (E.coli) type 1 fimbriae adhere to avian tracheal epithelial cells through the FimH protein. However, the adhesion-related antigen is still unknown. The purpose of this study was to analyze the antigenicity of the type 1 fimbrial FimH protein of wild-type avian E. coli, screen antigen epitopes, and prepare monoclonal antibodies (mAbs) that can block the adhesion of avian E. coli.

resultsIn this study, the nucleic acid homologies of MG2 (O11), TS12 (O18), and YR5 (O78) with K12 were 97.7%, 99.6%, and 97.7%, respectively, and the amino acid sequence similarity reached 98.7%, 99.3%, and 98.0%, respectively. The epitopes and hydrophilicities of the FimH proteins of these three strains were similar. The more obvious lectin domain epitopes were located at FimH protein positions 111-124 and 154-162. The mAbs 7C2 and 7D8 against these two epitopes were prepared. An adhesion inhibition test showed that 7C2 and 7D8 blocked bacterial adhesion to avian tracheal epithelial cells. The mAb 7C2 against the 111-124 epitope inhibited O78 strain adhesion by 93%, and the mAb 7D8 against the 154-162 epitope inhibited O78 strain adhesion by 49%, indicating that these two epitopes are closely related to the adhesion of type 1 fimbriae. However, only the 111-124 epitope-recognizing mAb 7C2 inhibited bacterial agglutination of erythrocytes, indicating that host cell receptor binding and erythrocyte agglutination are not mediated by the same spatial locations within the FimH protein.

conclusionsThe results demonstrate that the mAbs 7C2 and 7D8 against FimH protein positions 111-124 and 154-162 could inhibit the adhesion of E.coli to the chicken trachea.

Indexed as

Escherichia coliFimbriae ProteinsAdhesins, Escherichia coliAgglutininsAnimalsBacterial AdhesionEpitopesAdhesins, Escherichia coliAgglutininsEpitopesFimbriae ProteinsAdhesionAntigenic epitopeFimH proteinLectin domainType 1 fimbriae

Identifiers

PMID37789311
PMCPMC10546689
OpenAlexW4387302663

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.