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Adjuvant effect of B domain of staphyloccocal protein A displayed on the surface of hepatitis B virus capsid
Author(s) -
Kim Hyun Jin,
Ahn KeumYoung,
Bae Kyung Dong,
Lee Jiyun,
Sim Sang Jun,
Lee Jeewon
Publication year - 2016
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.25716
Subject(s) - adjuvant , hepatitis b virus , capsid , immune system , virology , antigen , cytotoxic t cell , antibody , biology , recombinant dna , virus like particle , t cell , microbiology and biotechnology , virus , chemistry , immunology , in vitro , biochemistry , gene
The hepatitis B virus (HBV) capsid‐based recombinant particles, which display both major hydrophilic region of HBV surface antigen (HBV–MHR) and B domain of Staphylococcal protein A (SPA B ), were produced using Escherichia coli as expression host. SPA B was used as an adjuvant to elicit the immune response to HBV–MHR, and its adjuvant effect in the immunized mice was estimated with varying the position and amount of SPA B on the HBV capsid particles. Compared to the emulsified aluminum gel (alum gel) that is a currently commercialized vaccine adjuvant, SPA B caused the significantly higher level of anti‐HBV immunoglobulin G (IgG) titer and seroconversion rate, and notably SPA B at the most surface‐exposed position on the recombinant particle led to the highest immune response. Moreover, SPA B caused much lower ratio of IgG1 to IgG2a compared to alum gel, indicating that helper T‐cell 1‐mediated immune response (responsible for cytotoxic T‐cell stimulation) is relatively more stimulated by SPA B , unlike alum gel that mainly stimulates helper T‐cell 2‐mediated immune response (responsible for B‐cell stimulation). Although HBV–MHR and HBV capsid particle were used as proof‐of‐concept in this study, SPA B can be used as a highly effective adjuvant with other disease‐specific antigens on the surface of other virus‐like particles to produce various recombinant vaccines with high potency. Biotechnol. Bioeng. 2016;113: 268–274. © 2015 Wiley Periodicals, Inc.