ArticlePloS one2010
An influenza A/H1N1/2009 hemagglutinin vaccine produced in Escherichia coli.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 65 citations in OpenAlex.
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- Production of Influenza Virus Glycoproteins Using Insect Cells.Methods in molecular biology (Clifton, N.J.) · 2024Article
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- Immunoinformatic analysis of the whole proteome for vaccine design: An application toFrontiers in immunology · 2022Article
- Designing a multi-epitope vaccine to provoke the robust immune response against influenza A H7N9.Scientific reports · 2021Article
- Unique features of a recombinant haemagglutinin influenza vaccine that influence vaccine performance.NPJ vaccines · 2021Review
- Animal Cell Expression Systems.Advances in biochemical engineering/biotechnology · 2021Article
- Influenza Hemagglutinin Head Domain Mimicry by Rational Design.The protein journal · 2020Article
- 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
- A Systematic Protein Refolding Screen Method using the DGR Approach Reveals that Time and Secondary TSA are Essential Variables.Scientific reports · 2017Article
- Vaccination with Killed but Metabolically ActiveJournal of nature and science · 2017Article
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- Characterization of Influenza Vaccine Hemagglutinin Complexes by Cryo-Electron Microscopy and Image Analyses Reveals Structural Polymorphisms.Clinical and vaccine immunology : CVI · 2016Article
- Advances in the development of influenza virus vaccines.Nature reviews. Drug discovery · 2015Review
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- Preliminary study about sublingual administration of bacteria-expressed pandemic H1N1 influenza vaccine in miniature pigs.Journal of microbiology (Seoul, Korea) · 2014Article
- Article
Corrections and comments
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Authors and funding
19 authors at 2 institutions in 2 countries.
Funding
Abstract
backgroundThe A/H1N1/2009 influenza pandemic made evident the need for faster and higher-yield methods for the production of influenza vaccines. Platforms based on virus culture in mammalian or insect cells are currently under investigation. Alternatively, expression of fragments of the hemagglutinin (HA) protein in prokaryotic systems can potentially be the most efficacious strategy for the manufacture of large quantities of influenza vaccine in a short period of time. Despite experimental evidence on the immunogenic potential of HA protein constructs expressed in bacteria, it is still generally accepted that glycosylation should be a requirement for vaccine efficacy. METHODOLOGY/PRINCIPAL
findingsWe expressed the globular HA receptor binding domain, referred to here as HA(63-286)-RBD, of the influenza A/H1N1/2009 virus in Escherichia coli using a simple, robust and scalable process. The recombinant protein was refolded and purified from the insoluble fraction of the cellular lysate as a single species. Recombinant HA(63-286)-RBD appears to be properly folded, as shown by analytical ultracentrifugation and bio-recognition assays. It binds specifically to serum antibodies from influenza A/H1N1/2009 patients and was found to be immunogenic, to be capable of triggering the production of neutralizing antibodies, and to have protective activity in the ferret model. CONCLUSIONS/SIGNIFICANCE: Projections based on our production/purification data indicate that this strategy could yield up to half a billion doses of vaccine per month in a medium-scale pharmaceutical production facility equipped for bacterial culture. Also, our findings demonstrate that glycosylation is not a mandatory requirement for influenza vaccine efficacy.
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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.