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

Highlights•HBsAg is an α/β protein quite stable to pH treatment (from 5.5 to 8.5). •Temperatures higher than 45 °C might promote some level of HBsAg unfolding. •Fully HBsAg denaturation with loss of its antigenicity properties occurs at 100 °C. •HBsAg vaccine stability is preserved even after 6 mont...

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Veröffentlicht in:	Vaccine 2019-10, Vol.37 (43), p.6415-6425
Hauptverfasser:	Lopes, J.L.S, Oliveira, D.C.A, Utescher, C.L.A, Quintilio, W, Tenório, E.C.N, Oliveira, C.L.P, Fantini, M.C.A, Rasmussen, M.K, Bordallo, H.N, Sant'Anna, O.A, Botosso, V.F
Format:	Artikel
Sprache:	eng
Schlagworte:	Allergy and Immunology Aluminum Antigens Circular dichroism Combined vaccines Dichroism Drug delivery systems Experiments Extreme values Fluorescence HBsAg antigenicity Hepatitis Hepatitis B Hepatitis B surface antigen High temperature Immune system Immunization Ionic strength Melting point Melting points Morphology pH effects pH stability Protein structure Proteins Resonance scattering Secondary structure Silica Silicon dioxide Small angle X ray scattering Stability Storage temperature Surface plasmon resonance Synchrotron radiation Temperature effects Thermal stability Vaccines Viruses X-ray scattering
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Zusammenfassung:	Highlights•HBsAg is an α/β protein quite stable to pH treatment (from 5.5 to 8.5). •Temperatures higher than 45 °C might promote some level of HBsAg unfolding. •Fully HBsAg denaturation with loss of its antigenicity properties occurs at 100 °C. •HBsAg vaccine stability is preserved even after 6 months storage.
ISSN:	0264-410X 1873-2518
DOI:	10.1016/j.vaccine.2019.09.005