Unknown

Dataset Information

0

Versatile virus-like particle carrier for epitope based vaccines.


ABSTRACT:

Background

Recombinant proteins and in particular single domains or peptides are often poorly immunogenic unless conjugated to a carrier protein. Virus-like-particles are a very efficient means to confer high immunogenicity to antigens. We report here the development of virus-like-particles (VLPs) derived from the RNA bacteriophage AP205 for epitope-based vaccines.

Methodology/principal findings

Peptides of angiotensin II, S.typhi outer membrane protein (D2), CXCR4 receptor, HIV1 Nef, gonadotropin releasing hormone (GnRH), Influenza A M2-protein were fused to either N- or C-terminus of AP205 coat protein. The A205-peptide fusions assembled into VLPs, and peptides displayed on the VLP were highly immunogenic in mice. GnRH fused to the C-terminus of AP205 induced a strong antibody response that inhibited GnRH function in vivo. Exposure of the M2-protein peptide at the N-terminus of AP205 resulted in a strong M2-specific antibody response upon immunization, protecting 100% of mice from a lethal influenza infection.

Conclusions/significance

AP205 VLPs are therefore a very efficient and new vaccine system, suitable for complex and long epitopes, of up to at least 55 amino acid residues in length. AP205 VLPs confer a high immunogenicity to displayed epitopes, as shown by inhibition of endogenous GnRH and protective immunity against influenza infection.

SUBMITTER: Tissot AC 

PROVIDER: S-EPMC2843720 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications


<h4>Background</h4>Recombinant proteins and in particular single domains or peptides are often poorly immunogenic unless conjugated to a carrier protein. Virus-like-particles are a very efficient means to confer high immunogenicity to antigens. We report here the development of virus-like-particles (VLPs) derived from the RNA bacteriophage AP205 for epitope-based vaccines.<h4>Methodology/principal findings</h4>Peptides of angiotensin II, S.typhi outer membrane protein (D2), CXCR4 receptor, HIV1  ...[more]

Similar Datasets

| S-EPMC4627648 | biostudies-literature
| S-EPMC4341857 | biostudies-literature
| S-EPMC7115488 | biostudies-literature
| S-EPMC7496916 | biostudies-literature
| S-EPMC7019592 | biostudies-literature
| S-EPMC5215943 | biostudies-literature
| S-EPMC4688205 | biostudies-literature
| S-EPMC7161758 | biostudies-literature
| S-EPMC7765226 | biostudies-literature
| S-EPMC4054422 | biostudies-literature