Evidence map›Paper›PMID 28456726›Full record

ArticleJournal of pharmaceutical sciences2017

Optimization of the Production Process and Characterization of the Yeast-Expressed SARS-CoV Recombinant Receptor-Binding Domain (RBD219-N1), a SARS Vaccine Candidate.

Wen-Hsiang Chen, Shivali M Chag, Mohan V Poongavanam, Amadeo B Biter, Ebe A Ewere, Wanderson Rezende, Christopher A Seid, Elissa M Hudspeth, Jeroen Pollet, C Patrick McAtee and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of pharmaceutical sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
11.6field-weighted citation impact, top 1% 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

55 citing papers in PubMed, 115 citations in OpenAlex.

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  12. Healthcare Innovations to Address the Challenges of the COVID-19 Pandemic.IEEE journal of biomedical and health informatics · 2022
    Article
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  16. Frontiers in bioengineering and biotechnology · 2022
    Review
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  19. Review
  20. Engineered SARS-CoV-2 receptor binding domain improves manufacturability in yeast and immunogenicity in mice.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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

13 authors at 3 institutions in 1 country.

Wen-Hsiang ChenTexas Children's Hospital Center for Vaccine Development, Houston, Texas 77030.
Shivali M ChagTexas Children's Hospital Center for Vaccine Development, Houston, Texas 77030.
Mohan V PoongavanamTexas Children's Hospital Center for Vaccine Development, Houston, Texas 77030.
Amadeo B BiterTexas Children's Hospital Center for Vaccine Development, Houston, Texas 77030.
Ebe A EwereTexas Children's Hospital Center for Vaccine Development, Houston, Texas 77030.
Wanderson RezendeTexas Children's Hospital Center for Vaccine Development, Houston, Texas 77030.
Christopher A SeidTexas Children's Hospital Center for Vaccine Development, Houston, Texas 77030.
Elissa M HudspethTexas Children's Hospital Center for Vaccine Development, Houston, Texas 77030.
Jeroen PolletTexas Children's Hospital Center for Vaccine Development, Houston, Texas 77030; Department of Pediatrics, National School of Tropical Medicine, Baylor College of Medicine, Houston, Texas 77030; Department of Molecular Virology and Microbiology, National School of Tropical Medicine, Baylor College of Medicine, Houston, Texas 77030.
C Patrick McAteeTexas Children's Hospital Center for Vaccine Development, Houston, Texas 77030.
Ulrich StrychTexas Children's Hospital Center for Vaccine Development, Houston, Texas 77030; Department of Pediatrics, National School of Tropical Medicine, Baylor College of Medicine, Houston, Texas 77030; Department of Molecular Virology and Microbiology, National School of Tropical Medicine, Baylor College of Medicine, Houston, Texas 77030.
Maria Elena BottazziTexas Children's Hospital Center for Vaccine Development, Houston, Texas 77030; Department of Pediatrics, National School of Tropical Medicine, Baylor College of Medicine, Houston, Texas 77030; Department of Molecular Virology and Microbiology, National School of Tropical Medicine, Baylor College of Medicine, Houston, Texas 77030; Department of Biology, Baylor University, Waco, Texas 76798. Electronic address: bottazzi@bcm.edu.
Peter J HotezTexas Children's Hospital Center for Vaccine Development, Houston, Texas 77030; Department of Pediatrics, National School of Tropical Medicine, Baylor College of Medicine, Houston, Texas 77030; Department of Molecular Virology and Microbiology, National School of Tropical Medicine, Baylor College of Medicine, Houston, Texas 77030; Department of Biology, Baylor University, Waco, Texas 76798; James A. Baker III Institute for Public Policy, Rice University, Houston, Texas 77005.
Texas Children's Hospital · USBaylor College of Medicine · USRice University · US

Funding

RBD recombinant protein-based SARS vaccine for biodefenseR01AI098775 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI BOTTAZZI, MARIA ELENA, HOTEZ, PETER J · 2012 to 2016
$6.1M
NIAID NIH HHS R01 AI098775
6 · The paper itself

Abstract

From 2002 to 2003, a global pandemic of severe acute respiratory syndrome (SARS) spread to 5 continents and caused 8000 respiratory infections and 800 deaths. To ameliorate the effects of future outbreaks as well as to prepare for biodefense, a process for the production of a recombinant protein vaccine candidate is under development. Previously, we reported the 5 L scale expression and purification of a promising recombinant SARS vaccine candidate, RBD219-N1, the 218-amino acid residue receptor-binding domain (RBD) of SARS coronavirus expressed in yeast-Pichia pastoris X-33. When adjuvanted with aluminum hydroxide, this protein elicited high neutralizing antibody titers and high RBD-specific antibody titers. However, the yield of RBD219-N1 (60 mg RBD219-N1 per liter of fermentation supernatant; 60 mg/L FS) still required improvement to reach our target of >100 mg/L FS. In this study, we optimized the 10 L scale production process and increased the fermentation yield 6- to 7-fold to 400 mg/L FS with purification recovery >50%. A panel of characterization tests indicated that the process is reproducible and that the purified, tag-free RBD219-N1 protein has high purity and a well-defined structure and is therefore a suitable candidate for production under current Good Manufacturing Practice and future phase-1 clinical trials.

Indexed as

Cloning, MolecularFermentationHumansIndustrial MicrobiologyPichiaProtein DomainsRecombinant ProteinsSevere Acute Respiratory SyndromeSevere acute respiratory syndrome-related coronavirusSpike Glycoprotein, CoronavirusVaccines, SyntheticViral VaccinesRecombinant ProteinsSpike Glycoprotein, Coronavirusspike glycoprotein, SARS-CoVVaccines, SyntheticViral Vaccinescircular dichroismhydrophobic interaction chromatographyPichia pastorisprotein characterizationprotein purification

Identifiers

PMID28456726
PMCPMC5612335
OpenAlexW2609522093

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.