Virology Journal

official impact factor 2.55

Open Access Research

Characterization of a branched lipopeptide candidate vaccine against influenza A/Puerto Rico 8/34 which is recognized by human B and T-cell immune responses

Liz Samayoa1,3, Francisco Diaz-Mitoma2,4 and Ali Azizi1,2*

Author Affiliations

1 Infectious Disease and Vaccine Research Center, Children's Hospital of Eastern Ontario Research Institute, 401 Smyth Rd, Ottawa, ON, K1H 8L1, Canada

2 Department of Pathology and Laboratory Medicine, University of Ottawa, 451 Smyth Rd, Ottawa, ON, K1H 8M5, Canada

3 Department of Microbiology and Immunology, University of Ottawa, 451 Smyth Rd, Ottawa, Ontario, K1H 8M5, Canada

4 Sudbury Regional Hospital Foundation, 41 Ramsey Lake Road, Sudbury, ON, P3E 5J1, Canada

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Virology Journal 2011, 8:309 doi:10.1186/1743-422X-8-309

Published: 16 June 2011

Abstract

The use of synthetic peptides as immunogens represents an exciting alternative to traditional vaccines. However, to date most of these synthetic peptides are not highly immunogenic. The lack of immunogenicity might be addressed by conjugation between T or B cell epitopes with universal or immunodominant T-helper epitopes. The construction of lipidated peptides, branched peptides, or designs combining both of these elements might enhance the immunogenicity, as they might target Toll-Like Receptors and/or mimic the 3-dimensional structure of epitopes within the native protein. Herein, a recognized peptide immunogen based on the hemagglutinin protein of A/Puerto Rico/8/34 was chosen as a backbone and modified to evaluate if the construction of branched peptides, lipidation, the addition of cysteine residues, or mutations could indeed alter epitope reactivity. Screening the different designs with various antibody binding and cellular assays revealed that combining a branched design with the addition of lipid moieties greatly enhanced the immunoreactivity.