Induction of Antigen-Specific CTL Responses Using Antigens Conjugated to Short Peptide Vectors

Day, Fiona H.; Clair, Philippe; Grabstein, Kenneth H.; Mazel, Martine; Rees, Anthony R.; Kaczorek, Michel; Temsamani, Jamal

doi:10.4049/jimmunol.170.3.1498

Cited by 8 publications

(2 citation statements)

References 46 publications

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“…Sera were evaluated at a screening dilution of 1:200. (30). The sequence of the J and G ICBL/TCBL and their lack of extensive portions or regions of basic amino acids also argues against an action similar to the SynB vectors which enhance the transport of SynB conjugates across the cell membranes (31,32,33), or cell entry via the beta defensin route (34).…”

Section: Comparsion With Other Epitope Delivery Technologiesmentioning

confidence: 99%

The L.E.A.P.S. approach to vaccine development

Zimmerman¹

2005

Front Biosci

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The Ligand Epitope Antigen Presentation System (L.E.A.P.S.) approach to vaccine development utilizes immune peptides to promote the immunogenicity and influence the type of immune response generated towards epitopes in peptides which may be too small to elicit an immune response. The covalent attachment of these immune peptides to the antigenic peptide promotes the interaction of the epitope with T cells (T cell binding ligand (TCBL)) or antigen presenting cells (immune cell binding ligand (ICBL)) and ultimately promotes binding with the T cell receptor on CD4 or CD8 T cells. The, J, ICBL/TCBL peptide derived from the beta-2-microglobulin chain of MHC I molecules promotes Th1 type responses to the antigenic peptide while the, G, ICBL/TCBL peptide derived from the beta chain of MHC II molecules promotes Th2 types of responses. The efficacy of this approach has been demonstrated by characterization of the immune responses to L.E.A.P.S. vaccines and by elicitation of protection from infectious challenge with herpes simplex virus and other pathogens. The protection studies show that the L.E.A.P.S. approach allows customization of the immune response appropriate for inducing protection from disease. The theory, background, examples and studies of the mechanism of action of the L.E.A.P.S. vaccines will be discussed.

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Section: Comparsion With Other Epitope Delivery Technologiesmentioning

confidence: 99%

The L.E.A.P.S. approach to vaccine development

Zimmerman¹

2005

Front Biosci

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“…Soluble polypeptides are very bad immunogens for eliciting cellular responses. In general, subunit Ag need potent adjuvants to improve their immunogenicity, even when results show the delivery of exogenous proteins into cells using membrane permeable carrier peptides 32 , 33 . Nonetheless, the conjugation step is an important drawback in this approach.…”

Section: Introductionmentioning

confidence: 99%

Coinoculation with hepatitis B surface and core antigen promotes a Th1 immune response to a multiepitopic protein of HIV‐1

et al. 2006

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Summary It has been defined that strong and multispecific cellular immune responses correlate with a better prognosis during the course of chronic diseases. A cross-enhancing effect on the resulting immune response obtained by the coadministration of recombinant hepatitis B virus (HBV) surface and core Ag was recently observed. With the objective of studying the effect of such Ag on the immune response to coinoculated heterologous Ag and vice versa, several formulations containing the recombinant HBVAg and a multiepitopic protein (CR3) composed by CTL and Th epitopes from HIV-1 were evaluated by s.c. and mucosal administration. Combinations of two and three Ag were evaluated for cellular and humoral immune responses. The results showed that the best Ag combination for nasal immunization was the mixture comprising the CR3 recombinant HIV protein and both HBV Ag. Similarly, it was also the best formulation for s.c. immunization in aluminium phosphate adjuvant. In conclusion, it is possible to induce a Th1 stimulation of the cellular immune response specific for a HIV-based recombinant protein by formulating this Ag with the recombinant HBV Ag.

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Peptides containing antigenic and cationic domains have enhanced, multivalent immunogenicity when bound to DNA vaccines

Riedl

Reimann

Schirmbeck

2004

Journal of Molecular Medicine

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We explored strategies to codeliver DNA- and peptide-based vaccines in a way that enhances the immunogenicity of both components of the combination vaccine for T cells. Specific CD8(+) T cell responses to an antigenic peptide are primed when the peptide is fused to a cationic peptide domain that is bound to plasmid DNA or oligonucleotides (ODN; with or without CpG motifs). Plasmid DNA mixed with antigenic/cationic peptides or histones forms large complexes with different biological properties depending on the molar ratios of peptide/protein and polynucleotide. Complexes containing high (but not low) molar ratios of cationic peptide to DNA facilitate transfection (DNA uptake and expression of the plasmid-encoded product) of cells. In contrast, complexes containing low (but not high) molar ratios of cationic peptide to DNA prime potent multispecific T cell responses after a single intramuscular injection of the complexes. The general validity of this observation was confirmed mixing different antigenic/cationic peptides with different DNA vaccines. In these vaccine formulations, multispecific CD8(+) T cell responses specific for epitopes of the peptide- as well as the DNA-based vaccine were efficiently coprimed, together with humoral antibody responses to conformational determinants of large viral antigens encoded by the DNA vaccine. The data indicate that mixtures of DNA vaccines with antigenic, cationic peptides are immunogenic vaccine formulations particularly suited for the induction of multispecific T cell responses.

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Induction of Antigen-Specific CTL Responses Using Antigens Conjugated to Short Peptide Vectors

Cited by 8 publications

References 46 publications

The L.E.A.P.S. approach to vaccine development

The L.E.A.P.S. approach to vaccine development

Coinoculation with hepatitis B surface and core antigen promotes a Th1 immune response to a multiepitopic protein of HIV‐1

Peptides containing antigenic and cationic domains have enhanced, multivalent immunogenicity when bound to DNA vaccines

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