ArticleBiotechnology and bioengineering2012
Cell-free production of trimeric influenza hemagglutinin head domain proteins as vaccine antigens.
Article in Biotechnology and bioengineering, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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.
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.
Who cites it
16 citing papers in PubMed, 37 citations in OpenAlex.
- International multisite implementation of distributed cell-free protein biomanufacturing to advance health and research equity.Science advances · 2026Article
- Review
- Toward efficient multiple-site incorporation of unnatural amino acids using cell-free translation system.Synthetic and systems biotechnology · 2022Article
- Best Practices for DNA Template Preparation Toward Improved Reproducibility in Cell-Free Protein Production.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Effects of DNA template preparation on variability in cell-free protein production.Synthetic biology (Oxford, England) · 2022Article
- Cell-Free Expression of a Plant Membrane Protein BrPT2 From Boesenbergia Rotunda.Molecular biotechnology · 2021Article
- Effective Use of Linear DNA in Cell-Free Expression Systems.Frontiers in bioengineering and biotechnology · 2021Review
- Streamlining the preparation of "endotoxin-free" ClearColi cell extract with autoinduction media for cell-free protein synthesis of the therapeutic protein crisantaspase.Synthetic and systems biotechnology · 2019Article
- Synthetic Biology Goes Cell-Free.BMC biology · 2019Review
- Exploring the Potential of Cell-Free Protein Synthesis for Extending the Abilities of Biological Systems.Frontiers in bioengineering and biotechnology · 2019Review
- Perspective: Solidifying the impact of cell-free synthetic biology through lyophilization.Biochemical engineering journal · 2018Article
- Harnessing an RNA-mediated chaperone for the assembly of influenza hemagglutinin in an immunologically relevant conformation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
- Cell-free synthetic biology: Engineering in an open world.Synthetic and systems biotechnology · 2017Review
- Functional properties of flagellin as a stimulator of innate immunity.Scientific reports · 2016Article
- Advances in the development of influenza virus vaccines.Nature reviews. Drug discovery · 2015Review
- Vaccine design: emerging concepts and renewed optimism.Current opinion in biotechnology · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
In order to effectively combat pandemic influenza threats, there is a need for more rapid and robust vaccine production methods. In this article, we demonstrate E. coli-based cell-free protein synthesis (CFPS) as a method to rapidly produce domains from the protein hemagglutinin (HA), which is present on the surface of the influenza virus. The portion of the HA coding sequence for the "head" domain from the 2009 pandemic H1N1 strain was first optimized for E. coli expression. The protein domain was then produced in CFPS reactions and purified in soluble form first as a monomer and then as a trimer by a C-terminal addition of the T4 bacteriophage foldon domain. Production of soluble trimeric HA head domain was enhanced by introducing stabilizing amino acid mutations to the construct in order to avoid aggregation. Trimerization was verified using size exclusion HPLC, and the stabilized HA head domain trimer was more effectively recognized by antibodies from pandemic H1N1 influenza vaccine recipients than was the monomer and also bound to sialic acids more strongly, indicating that the trimers are correctly formed and could be potentially effective as vaccines.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.