Evidence map›Paper›PMID 34087220›Full record

ArticlePeptides2021

Synthetic proteins for COVID-19 diagnostics.

Catherine H Schein, Corri B Levine, Susan L F McLellan, Surendra S Negi, Werner Braun, Stephen C Dreskin, Elizabeth S Anaya, Jurgen Schmidt

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Peptides, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. 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 at 3 institutions in 1 country.

Catherine H ScheinDepartment of Biochemistry and Molecular Biology, The University of Texas Medical Branch, Galveston, TX, United States; Institute for Human Infections and immunity (IHII), The University of Texas Medical Branch, Galveston, TX, United States. Electronic address: chschein@utmb.edu.
Corri B LevineInstitute for Translational Sciences, The University of Texas Medical Branch, Galveston, TX, United States.
Susan L F McLellanDepartment of Internal medicine - Infectious Diseases, The University of Texas Medical Branch, Galveston, TX, United States.
Surendra S NegiDepartment of Biochemistry and Molecular Biology, The University of Texas Medical Branch, Galveston, TX, United States; Sealy Center for Structural Biology and Molecular Biophysics, The University of Texas Medical Branch, Galveston, TX, United States.
Werner BraunDepartment of Biochemistry and Molecular Biology, The University of Texas Medical Branch, Galveston, TX, United States; Institute for Human Infections and immunity (IHII), The University of Texas Medical Branch, Galveston, TX, United States; Sealy Center for Structural Biology and Molecular Biophysics, The University of Texas Medical Branch, Galveston, TX, United States.
Stephen C DreskinDivision of Allergy and Clinical Immunology, Department of Medicine, University of Colorado Denver, Aurora, CO, 80045, United States.
Elizabeth S AnayaB-11 Bioenergy and Biome Sciences, Bioscience Division Los Alamos National Laboratory, Los Alamos, NM, 87545, United States.
Jurgen SchmidtB-11 Bioenergy and Biome Sciences, Bioscience Division Los Alamos National Laboratory, Los Alamos, NM, 87545, United States.
The University of Texas Medical Branch at Galveston · USLos Alamos National Laboratory · USUniversity of Colorado Denver · US

Funding

Mosaic Immunogens as Multivalent Alphavirus VaccinesR01AI137332 · NIAID · UNIVERSITY OF TEXAS MED BR GALVESTON · PI BRAUN, WERNER A · 2018 to 2021
$1.9M
NIAID NIH HHS R01 AI137332
6 · The paper itself

Abstract

There is an urgent need for inexpensive, rapid and specific antigen-based assays to test for vaccine efficacy and detect infection with SARS-CoV-2 and its variants. We have identified a small, synthetic protein (JS7), representing a region of maximum variability within the receptor binding domain (RBD), which binds antibodies in sera from nine patients with PCR-verified COVID-19 of varying severity. Antibodies binding to either JS7 or the SARS-CoV-2 recombinant RBD, as well as those that disrupt binding between a fragment of the ACE2 receptor and the RBD, are proportional to disease severity and clinical outcome. Binding to JS7 was inhibited by linear peptides from the RBD interface with ACE2. Variants of JS7, such as E484K or N501Y, can be quickly synthesized in pure form in large quantities by automated methods. JS7 and related synthetic antigens can provide a basis for specific diagnostics for SARS-CoV-2 infections.

Indexed as

COVID-19COVID-19 Serological TestingSARS-CoV-2Angiotensin-Converting Enzyme 2HumansPeptidesProtein DomainsSpike Glycoprotein, CoronavirusACE2 protein, humanAngiotensin-Converting Enzyme 2PeptidesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2ACE2 interactionCOVID-19 variantsNeutralizing antibodiesPeptide vaccinesReceptor binding domainS protein epitopesStructure based design

Identifiers

PMID34087220
PMCPMC8168367
OpenAlexW3164304251

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.