Evidence map›Paper›PMID 33731300›Full record

ArticleBiochimica et biophysica acta. General subjects2021

Genetic modification to design a stable yeast-expressed recombinant SARS-CoV-2 receptor binding domain as a COVID-19 vaccine candidate.

Wen-Hsiang Chen, Junfei Wei, Rakhi Tyagi Kundu, Rakesh Adhikari, Zhuyun Liu, Jungsoon Lee, Leroy Versteeg, Cristina Poveda, Brian Keegan, Maria Jose Villar and 8 more

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta. General subjects, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

41 citing papers in PubMed, 71 citations in OpenAlex.

  1. Trial
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  9. Backstage Heroes-Yeast in COVID-19 Research.International journal of molecular sciences · 2024
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Production and Immunogenicity Assessment of LTp50: AnPharmaceuticals (Basel, Switzerland) · 2024
    Article
  15. Article
  16. Efficient Expression inMolecules (Basel, Switzerland) · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. 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

18 authors at 3 institutions in 1 country.

Wen-Hsiang ChenTexas Children's Hospital Center for Vaccine Development, Houston, TX, USA; Departments of Pediatrics and Molecular Virology & Microbiology, National School of Tropical Medicine, Baylor College of Medicine, Houston, TX, USA.
Junfei WeiTexas Children's Hospital Center for Vaccine Development, Houston, TX, USA.
Rakhi Tyagi KunduTexas Children's Hospital Center for Vaccine Development, Houston, TX, USA.
Rakesh AdhikariTexas Children's Hospital Center for Vaccine Development, Houston, TX, USA.
Zhuyun LiuTexas Children's Hospital Center for Vaccine Development, Houston, TX, USA.
Jungsoon LeeTexas Children's Hospital Center for Vaccine Development, Houston, TX, USA.
Leroy VersteegTexas Children's Hospital Center for Vaccine Development, Houston, TX, USA.
Cristina PovedaTexas Children's Hospital Center for Vaccine Development, Houston, TX, USA.
Brian KeeganTexas Children's Hospital Center for Vaccine Development, Houston, TX, USA.
Maria Jose VillarTexas Children's Hospital Center for Vaccine Development, Houston, TX, USA.
Ana C de Araujo LeaoTexas Children's Hospital Center for Vaccine Development, Houston, TX, USA.
Joanne Altieri RiveraTexas Children's Hospital Center for Vaccine Development, Houston, TX, USA.
Portia M GillespieTexas Children's Hospital Center for Vaccine Development, Houston, TX, USA.
Jeroen PolletTexas Children's Hospital Center for Vaccine Development, Houston, TX, USA; Departments of Pediatrics and Molecular Virology & Microbiology, National School of Tropical Medicine, Baylor College of Medicine, Houston, TX, USA.
Ulrich StrychTexas Children's Hospital Center for Vaccine Development, Houston, TX, USA; Departments of Pediatrics and Molecular Virology & Microbiology, National School of Tropical Medicine, Baylor College of Medicine, Houston, TX, USA.
Bin ZhanTexas Children's Hospital Center for Vaccine Development, Houston, TX, USA; Departments of Pediatrics and Molecular Virology & Microbiology, National School of Tropical Medicine, Baylor College of Medicine, Houston, TX, USA.
Peter J HotezTexas Children's Hospital Center for Vaccine Development, Houston, TX, USA; Departments of Pediatrics and Molecular Virology & Microbiology, National School of Tropical Medicine, Baylor College of Medicine, Houston, TX, USA; Department of Biology, Baylor University, Waco, TX, USA; James A. Baker III Institute for Public Policy, Rice University, Houston, TX, USA. Electronic address: hotez@bcm.edu.
Maria Elena BottazziTexas Children's Hospital Center for Vaccine Development, Houston, TX, USA; Departments of Pediatrics and Molecular Virology & Microbiology, National School of Tropical Medicine, Baylor College of Medicine, Houston, TX, USA; Department of Biology, Baylor University, Waco, TX, USA; James A. Baker III Institute for Public Policy, Rice University, Houston, TX, USA. Electronic address: bottazzi@bcm.edu.
Texas Children's Hospital · USBaylor College of Medicine · USBaylor University · US

Funding

Development of a safe and effective RBD-based vaccine against MERS-CoVR56AI140872 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI HOTEZ, PETER J · 2020 to 2020
$549k
NIAID NIH HHS R56 AI140872
6 · The paper itself

Abstract

backgroundCoronavirus disease 2019 (COVID-19) caused by SARS-CoV-2 has now spread worldwide to infect over 110 million people, with approximately 2.5 million reported deaths. A safe and effective vaccine remains urgently needed.

methodWe constructed three variants of the recombinant receptor-binding domain (RBD) of the SARS-CoV-2 spike (S) protein (residues 331-549) in yeast as follows: (1) a "wild type" RBD (RBD219-WT), (2) a deglycosylated form (RBD219-N1) by deleting the first N-glycosylation site, and (3) a combined deglycosylated and cysteine-mutagenized form (C538A-mutated variant (RBD219-N1C1)). We compared the expression yields, biophysical characteristics, and functionality of the proteins produced from these constructs. RESULTS AND

conclusionsThese three recombinant RBDs showed similar secondary and tertiary structure thermal stability and had the same affinity to their receptor, angiotensin-converting enzyme 2 (ACE-2), suggesting that the selected deletion or mutations did not cause any significant structural changes or alteration of function. However, RBD219-N1C1 had a higher fermentation yield, was easier to purify, was not hyperglycosylated, and had a lower tendency to form oligomers, and thus was selected for further vaccine development and evaluation. GENERAL SIGNIFICANCE: By genetic modification, we were able to design a better-controlled and more stable vaccine candidate, which is an essential and important criterion for any process and manufacturing of biologics or drugs for human use.

Indexed as

Amino Acid SequenceCloning, MolecularCOVID-19 VaccinesGene ExpressionProtein DomainsProtein Structure, TertiaryRecombinant ProteinsSaccharomycetalesSARS-CoV-2Spike Glycoprotein, CoronavirusCOVID-19 VaccinesRecombinant ProteinsSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2Biophysical characterizationBiotechnologyCoronavirusP. pastoris

Identifiers

PMID33731300
PMCPMC7955913
OpenAlexW3138276667

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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.