Efficient stabilization of therapeutic hepatitis B vaccine components by amino-acid formulation maintains its potential to break immune tolerance.
JHEP Rep
; 5(2): 100603, 2023 Feb.
Article
in En
| MEDLINE
| ID: mdl-36714793
AAV, adeno-associated virus; ALT, alanine aminotransferase; CHB, chronic hepatitis B; CTC, controlled temperature chain; Ctrl, control; DLS, dynamic light scattering; HBcAg; HBcAg, hepatitis B core antigen; HBeAg, hepatitis B e antigen; HBsAg; HBsAg, hepatitis B surface antigen; Heat-stable vaccine; ICS, intracellular cytokine staining; IFNα, interferon alpha; MVA; MVA, Modified Vaccinia virus Ankara; NAGE, native agarose gel electrophoresis; RH, relative humidity; RT, room temperature; SAA, stabilizing amino acids; SEC-HPLC, size exclusion-high performance liquid chromatography; SPS®; TCID50, median tissue culture infection dose; TherVacBCtrl, non-lyophilized; WHO, World Health Organization; anti-HBc, hepatitis B core antibodies; anti-HBs, hepatitis B surface antibodies; cccDNA, covalently closed circular DNA; formulation; hepatitis B virus; heterologous prime/boost vaccination; lyophilization; non-stressed, non-stabilized TherVacB; stabilization; stabilizing amino acid-based formulation; stabilizing excipients
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Language:
En
Journal:
JHEP Rep
Year:
2023
Document type:
Article
Affiliation country:
Alemania