Evidence map›Paper›PMID 29497069›Full record

ArticleScientific reports2018

A Highly Sensitive Detection System based on Proximity-dependent Hybridization with Computer-aided Affinity Maturation of a scFv Antibody.

Zhiheng Wang, Yan Li, Wenbin Liang, Junsong Zheng, Shuhui Li, Chuanmin Hu, An Chen

Abstract read
In one paragraph

Article in Scientific reports, 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
–field-weighted citation impact
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.

  1. Article
  2. Design of nanobody-based bispecific constructs byComputational and structural biotechnology journal · 2023
    Article
  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

7 authors.

Zhiheng WangDepartment of Clinical Biochemistry, College of Medical Laboratory, Southwest Hospital, Army Medical University (Third Military Medical University), 30 Gaotanyan Street, Shapingba District, Chongqing, 400038, PR China.
Yan LiDepartment of Clinical Laboratory Science, College of Medical Laboratory, Southwest Hospital, Army Medical University (Third Military Medical University), 30 Gaotanyan Street, Shapingba District, Chongqing, 400038, PR China.
Wenbin LiangDepartment of Clinical Biochemistry, College of Medical Laboratory, Southwest Hospital, Army Medical University (Third Military Medical University), 30 Gaotanyan Street, Shapingba District, Chongqing, 400038, PR China.
Junsong ZhengDepartment of Clinical Laboratory Science, College of Medical Laboratory, Southwest Hospital, Army Medical University (Third Military Medical University), 30 Gaotanyan Street, Shapingba District, Chongqing, 400038, PR China.
Shuhui LiDepartment of Clinical Biochemistry, College of Medical Laboratory, Southwest Hospital, Army Medical University (Third Military Medical University), 30 Gaotanyan Street, Shapingba District, Chongqing, 400038, PR China.
Chuanmin HuDepartment of Clinical Biochemistry, College of Medical Laboratory, Southwest Hospital, Army Medical University (Third Military Medical University), 30 Gaotanyan Street, Shapingba District, Chongqing, 400038, PR China.
An ChenDepartment of Clinical Biochemistry, College of Medical Laboratory, Southwest Hospital, Army Medical University (Third Military Medical University), 30 Gaotanyan Street, Shapingba District, Chongqing, 400038, PR China. chenan@tmmu.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The hepatitis B virus (HBV) infection is a critical health problem worldwide, and HBV preS1 is an important biomarker for monitoring HBV infection. Previously, we found that a murine monoclonal antibody, mAb-D8, targets the preS1 (aa91-107) fragment of HBV. To improve its performance, we prepared the single-chain variable region of mAb-D8 (scFvD8) and constructed the three-dimensional structure of the scFvD8-preS1 (aa91-107) complex by computer modelling. The affinity of scFvD8 was markedly increased by the introduction of mutations L96Tyr to Ser and H98Asp to Ser. Furthermore, a highly sensitive immunosensor was designed based on a proximity-dependent hybridization strategy in which the preS1 antigen competitively reacts with an antibody labelled with DNA, resulting in decreased proximity-dependent hybridization and increased electrochemical signal from the Fc fragment, which can be used for the quantisation of preS1. The results showed a wide detection range from 1 pM to 50 pM with a detection limit of 0.1 pM. The sensitivity and specificity of this immunosensor in clinical serum samples were 100% and 96%, respectively. This study provides a novel system based on proximity-dependent hybridization and the scFv antibody fragment for the rapid quantisation of antigens of interest with a high sensitivity.

Indexed as

Amino Acid SequenceAnimalsAntibodies, MonoclonalHepatitis BHepatitis B AntibodiesHepatitis B Surface AntigensHepatitis B virusHumansHybridomasMiceNucleic Acid HybridizationProtein PrecursorsSingle-Chain AntibodiesAntibodies, MonoclonalHepatitis B AntibodiesHepatitis B Surface Antigenspresurface protein 1, hepatitis B surface antigenProtein PrecursorsSingle-Chain Antibodies

Identifiers

PMID29497069
PMCPMC5832849

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Registered trials

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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.