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An Influenza A/H1N1/2009 hemagglutinin vaccine produced in Escherichia coli

dc.creatorRoberto Portillo Lara
dc.creatorJosé Manuel Aguilar Yáñez
dc.creatorMaría Yuriana Oropeza Almazán
dc.creatorMario Moisés Alvarez
dc.date2010
dc.date.accessioned2018-10-18T19:54:16Z
dc.date.available2018-10-18T19:54:16Z
dc.identifier.issn19326203
dc.identifier.doi10.1371/journal.pone.0011694
dc.identifier.urihttp://hdl.handle.net/11285/630272
dc.descriptionBackground: The 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 Findings: We expressed the globular HA receptor binding domain, referred to here as HA63-286 - 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 HA63-286 - 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. © 2010 Aguilar-Yáñez et al.
dc.languageeng
dc.relationhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-77955355550&doi=10.1371%2fjournal.pone.0011694&partnerID=40&md5=6d4152cd09420eef92edd06ca7213a07
dc.relationInvestigadores
dc.relationEstudiantes
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0
dc.sourcePLoS ONE
dc.subjecthemagglutinin 63-286
dc.subjectinfluenza vaccine
dc.subjectInfluenza virus hemagglutinin
dc.subjectneutralizing antibody
dc.subjectrecombinant protein
dc.subjectunclassified drug
dc.subjectinfluenza vaccine
dc.subjectvirus antibody
dc.subjectvirus hemagglutinin
dc.subjectanimal cell
dc.subjectanimal experiment
dc.subjectanimal model
dc.subjectantibody production
dc.subjectantigen binding
dc.subjectarticle
dc.subjectbioassay
dc.subjectcell lysate
dc.subjectcontrolled study
dc.subjectdose response
dc.subjectdrug binding
dc.subjectdrug dose comparison
dc.subjectdrug purification
dc.subjectEscherichia coli
dc.subjectferret
dc.subjecthuman
dc.subjectimmunogenicity
dc.subjectinfluenza A (H1N1)
dc.subjectInfluenza virus A H1N1
dc.subjectmolecular recognition
dc.subjectnonhuman
dc.subjectnucleotide sequence
dc.subjectprotein expression
dc.subjectprotein folding
dc.subjectprotein purification
dc.subjectsingle drug dose
dc.subjectultracentrifugation
dc.subjectvaccine production
dc.subjectanimal
dc.subjectblood
dc.subjectchemistry
dc.subjectenzyme linked immunosorbent assay
dc.subjectEscherichia coli
dc.subjectgenetics
dc.subjectimmunology
dc.subjectInfluenza virus A H1N1
dc.subjectmetabolism
dc.subjectreverse transcription polymerase chain reaction
dc.subjectAdolescent
dc.subjectAdult
dc.subjectAged
dc.subjectAged, 80 and over
dc.subjectAntibodies, Viral
dc.subjectAustralia
dc.subjectChild
dc.subjectChild, Preschool
dc.subjectCohort Studies
dc.subjectHumans
dc.subjectInfluenza A Virus, H1N1 Subtype
dc.subjectInfluenza, Human
dc.subjectMale
dc.subjectMiddle Aged
dc.subjectPandemics
dc.subjectSeasons
dc.subjectYoung Adult
dc.subjectAnimals
dc.subjectAntibodies, Viral
dc.subjectEnzyme-Linked Immunosorbent Assay
dc.subjectEscherichia coli
dc.subjectFerrets
dc.subjectHemagglutinins, Viral
dc.subjectInfluenza A Virus, H1N1 Subtype
dc.subjectInfluenza Vaccines
dc.subjectProtein Folding
dc.subjectReverse Transcriptase Polymerase Chain Reaction
dc.subjectBacteria (microorganisms)
dc.subjectEscherichia coli
dc.subjectHexapoda
dc.subjectMammalia
dc.subjectMustela
dc.subjectProkaryota
dc.subject.classification7 INGENIERÍA Y TECNOLOGÍA
dc.titleAn Influenza A/H1N1/2009 hemagglutinin vaccine produced in Escherichia coli
dc.typeArtículo
dc.identifier.volume5
dc.identifier.issue7
refterms.dateFOA2018-10-18T19:54:16Z


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