Antigenic and physicochemical characterization of Hepatitis B surface protein under extreme temperature and pH conditions

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dc.contributorLab. Virologiapt_BR
dc.contributorLab. Biofármacospt_BR
dc.contributorLab. Imunoquímicapt_BR
dc.contributor.authorLopes, J. L.S.pt_BR
dc.contributor.authorOliveira, Denise Cristina Andrépt_BR
dc.contributor.authorUtescher, Carla Lilian de Agostinipt_BR
dc.contributor.authorQuintilio, Wagnerpt_BR
dc.contributor.authorTenorio ECNpt_BR
dc.contributor.authorOliveira, C.L.P.pt_BR
dc.contributor.authorFantini, M.C.A.pt_BR
dc.contributor.authorRasmussen, M.K.pt_BR
dc.contributor.authorBordallo, H.N.pt_BR
dc.contributor.authorSant'Anna, Osvaldo Augusto Brazil Estevespt_BR
dc.contributor.authorBotosso, Viviane Fongaropt_BR
dc.date.accessioned2020-07-09T21:25:35Z-
dc.date.available2020-07-09T21:25:35Z-
dc.date.issued2019pt_BR
dc.identifier.citationLopes J.L.S., Oliveira DCA, Utescher CLA, Quintilio W, TECN, Oliveira C.L.P., et al. Antigenic and physicochemical characterization of Hepatitis B surface protein under extreme temperature and pH conditions. Vaccine. 2019 Oct;37(43):6415-6425. doi:10.1016/j.vaccine.2019.09.005.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/2868-
dc.description.abstractHepatitis B virus causes acute and chronic infections in millions of people worldwide and, since 1982, a vaccine with 95% effectiveness has been available for immunization. The main component of the recombinant hepatitis B vaccine is the surface antigen protein (HBsAg). In this work, the effect of pH, ionic strength and temperature on the native state of the HBsAg antigen were studied by a combination of biophysical methods that included small angle X-ray scattering, synchrotron radiation circular dichroism, fluorescence and surface plasmon resonance spectroscopies, as well as in vivo and in vitro potency assays. The native conformation, morphology, radius of gyration, and antigenic properties of the HBsAg antigen demonstrate high stability to pH treatment, especially in the pH range employed in all stages of HBsAg vaccine production and storage. The HBsAg protein presents thermal melting point close to 56°C, reaching a more unfolded state after crossing this point, but it only experiences loss of vaccine potency and antigenic properties at 100°C. Interestingly, a 6-month storage period does not affect vaccine stability, and the results are similar when the protein is kept under refrigerated conditions or at room temperature (20°C). At frozen temperatures, large aggregates (>200nm) are formed and possibly cause loss of HBsAg content, but that does not affect the in vivo assay. Furthermore, HBsAg has a well-ordered secondary structure content that is not affected when the protein is formulated with silica SBA-15, targeting the oral delivery of the vaccine. The combined results from all the characterization techniques employed in this study showed the high stability of the antigen at different storage temperature and extreme values of pH. These findings are important for considering the delivery of HBsAg to the immune system via an oral vaccine.pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorshipThe Danish Agency for Science, Technology and Innovationpt_BR
dc.format.extent6415-6425pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofVaccinept_BR
dc.rightsOpen Accesspt_BR
dc.titleAntigenic and physicochemical characterization of Hepatitis B surface protein under extreme temperature and pH conditionspt_BR
dc.typeArticlept_BR
dc.identifier.doi10.1016/j.vaccine.2019.09.005pt_BR
dc.identifier.urlhttps://doi.org/10.1016/j.vaccine.2019.09.005pt_BR
dc.contributor.externalUniversidade de São Paulo (USP)¦¦Brasilpt_BR
dc.contributor.externalUniversity of Copenhagen¦¦Dinamarcapt_BR
dc.contributor.externalUniversity of Denmark¦¦Dinamarcapt_BR
dc.contributor.externalEuropean Spallation Source (ESS)¦¦Suéciapt_BR
dc.identifier.citationvolume37pt_BR
dc.identifier.citationissue43pt_BR
dc.subject.keywordHepatitis Bpt_BR
dc.subject.keywordHBsAg antigenicitypt_BR
dc.subject.keywordThermal stabilitypt_BR
dc.subject.keywordpH stabilitypt_BR
dc.relation.ispartofabbreviatedVaccinept_BR
dc.identifier.citationabntv. 37, n. 43, p. 6415-6425, oct. 2019pt_BR
dc.identifier.citationvancouver2019 Oct;37(43):6415-6425pt_BR
dc.contributor.butantanOliveira, Denise Cristina André|:Pesquisador|:Lab. Virologia|:pt_BR
dc.contributor.butantanUtescher, Carla Lilian de Agostini|:Pesquisador|:Lab. Virologia|:pt_BR
dc.contributor.butantanQuintilio, Wagner|:Pesquisador|:Lab. Biofármacos |:pt_BR
dc.contributor.butantanTenorio ECN|:Pesquisador|:Lab. Virologia|:pt_BR
dc.contributor.butantanSant'Anna, Osvaldo Augusto Brazil Esteves|:Pesquisador|:Lab. Imunoquímica|:pt_BR
dc.contributor.butantanBotosso, Viviane Fongaro|:Pesquisador|:Lab. Virologia|:pt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦406429/2016-2pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2017/17844-8pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2018/19546-7pt_BR
dc.sponsorship.butantanThe Danish Agency for Science, Technology and Innovation¦¦5132-00054Bpt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
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