Evidence map›Paper›PMID 35642505›Full record

ArticlemSphere2022

Development of an Enzyme-Linked Immunosorbent Assay for Detection of the Native Conformation of Enterovirus A71.

Natalie J Kingston, Keith Grehan, Joseph S Snowden, Mona Shegdar, Helen Fox, Andrew J Macadam, David J Rowlands, Nicola J Stonehouse

Abstract read
In one paragraph

Article in mSphere, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. 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

8 authors.

Natalie J KingstonAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leedsgrid.9909.9, Leeds, United Kingdom.
Keith GrehanAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leedsgrid.9909.9, Leeds, United Kingdom.
Joseph S SnowdenAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leedsgrid.9909.9, Leeds, United Kingdom.ORCID 0000-0001-7857-0634
Mona ShegdarAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leedsgrid.9909.9, Leeds, United Kingdom.
Helen FoxDivision of Virology, National Institute for Biological Standards and Control, Potters Bar, Hertfordshire, United Kingdom.
Andrew J MacadamDivision of Virology, National Institute for Biological Standards and Control, Potters Bar, Hertfordshire, United Kingdom.
David J RowlandsAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leedsgrid.9909.9, Leeds, United Kingdom.ORCID 0000-0002-4742-9272
Nicola J StonehouseAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leedsgrid.9909.9, Leeds, United Kingdom.ORCID 0000-0003-1146-5519

Funding

Understanding the fundamental enterovirus capsid assembly and maturation pathway.R01AI169457 · NIAID · UNIVERSITY OF LEEDS · PI Nicola J Stonehouse · 2022 to 2026
$2.5M
Medical Research Council MR/P022626/1NIAID NIH HHS R01 AI169457Wellcome TrustWellcome Trust 102174/B/13/ZWellcome Trust 108466/Z/15/ZWellcome Trust 204825/Z/16/Z
6 · The paper itself

Abstract

Enterovirus A71 (EVA71) is a medically important virus that is commonly associated with hand, foot, and mouth disease (HFMD). It is responsible for periodic outbreaks, resulting in significant economic impact and loss of life. Vaccination offers the potential to control future outbreaks, and vaccine development has been increasingly the focus of global research efforts. However, antigenic characterization of vaccine candidates is challenging because there are few tools to characterize the different antigenic forms of the virus. As with other picornaviruses, EVA71 virions exist in two antigenic states, native (NAg) and expanded (HAg). It is likely that the composition of vaccines, in terms of the proportions of NAg and HAg, will be important for vaccine efficacy and batch-to-batch consistency. This paper describes the development of a single-chain fused variable (scFv) domain fragment and the optimization of a sandwich enzyme-linked immunosorbent assay (ELISA) for the specific detection of the NAg conformation of EVA71. NAg specificity of the scFv was demonstrated using purified EVA71, and conversion of NAg to HAg by heating resulted in a loss of binding. We have thus developed an effective tool for characterization of the specific antigenic state of EVA71.

Indexed as

EnterovirusEnterovirus InfectionsHand, Foot and Mouth DiseaseEnzyme-Linked Immunosorbent AssayHumansVaccinationenterovirus A71EVA71sandwich ELISAscFv

Identifiers

PMID35642505
PMCPMC9241546

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.