| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 3429563 | Virus Research | 2009 | 8 Pages |
The hepatitis B virus (HBV) surface small antigen (HBsAg) self-assembles into virus-like particles (VLPs). HBsAg-based VLPs constitute a powerful vector for heterologous immunogenic peptides to develop a safe vaccine delivery system. HBV and the human immunodeficiency virus type 1 (HIV-1) are frequently associated in infection. An HIV-1 class I polyepitope was designed for an HIV-1/HBV vaccine prototype based on HBsAg VLPs. Invariable peptides from the original HIV-1 polyepitope were here permutated to study the influence of epitope order on HIV-1/HBV VLP immunogenicity. Anti-HIV-1 cellular responses were statistically comparable among polyepitope variants. Nevertheless, delivered HIV-1 polyepitopes impacted anti-HBsAg carrier immunogenicity in a polyepitope-specific manner. For a given set of epitopes, the choice of epitope order in polyepitopes is strategic to control immune responses towards HBsAg VLPs used as carrier of foreign immunogenic peptides.
