Abstract
Peptides displayed on the surface of filamentous bacteriophage fd are able to induce humoral as well as cell-mediated immune responses, which makes phage particles an attractive antigen delivery system to design new vaccines. The immune response induced by phage-displayed peptides can be enhanced by targeting phage particles to the professional antigen presenting cells, utilizing a single-chain antibody fragment that binds dendritic cell receptor DEC-205. Here, we review recent advances in the use of filamentous phage fd as a platform for peptide vaccines, with a special focus on the use of phage fd as an antigen delivery platform for peptide vaccines in Alzheimer’s Disease and cancer.
Highlights
A crucial challenge for vaccine development is to design vaccines that induce long-lasting protective immune responses without compromising safety and tolerability
As solution NMR studies of the GPGRAF sequence embedded in 12 to 40 residue polypeptides failed to identify a persistent three-dimensional conformation [22], as is typically the case for short peptides in aqueous solution, this observation implies that a short peptide, when displayed on the bacteriophage coat protein, can in some instances have an enhanced propensity to adopt a conformation similar to that found in the native protein from which it is derived [22]
We have shown that fd virions displaying peptide RT2 (ILKEPVHGV), corresponding to residues 309–317 of the reverse transcriptase (RTase) of HIV-1, are able to prime a CTL response specific for this HIV-1 epitope in human cell lines [25]
Summary
A crucial challenge for vaccine development is to design vaccines that induce long-lasting protective immune responses without compromising safety and tolerability. It is important to focus the immune response to defined B and T epitopes, which in some instances consist of short peptides that are not, in themselves, immunogenic. Peptides can be chemically conjugated to the phage, or displayed as recombinant fusions to the coat proteins [2]. The immunogenicity of short peptide epitopes is enhanced when they are displayed on the phage capsid, chemical stability is increased [3], cloning and purification protocols required to produce the immunogen are easy, and costs are very low [4]. Phage-based products have been recently approved in food safety by the US. We discuss recent advances in the development of filamentous bacteriophage fd as an antigen delivery system for B and T cell epitopes. Bacteriophage fd shares a 98% identity with the genomes of filamentous phages M13 and f1
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