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Liposome entrapment and immunogenic studies of a synthetic lipophilic multiple antigenic peptide bearing VP1 and VP3 domains of the hepatitis A virus: a robust method for vaccine design

AuthorsHaro Villar, Isabel ; Pérez, Silvia; García, Mónica; Chan, Weng C.; Ercilla, Guadalupe
KeywordsHepatitis A virus
Multiple antigenic peptide
Peptide synthesis
Enzyme-linked immunosorbent assay
Surface plasmon resonance
Issue Date14-Mar-2003
CitationFEBS Letters 340(1-3): 133-140 (2003)
AbstractMultiple antigen peptides (MAP) have been demonstrated to be efficient immunological reagents for the induction of immune responses to a variety of infectious agents. Several peptide domains of the hepatitis A virus (HAV) capsid proteins, mainly VP1 and VP3, are the immunodominant targets for a protective antibody response. In the present study we analyse the immunogenic properties of a tetrameric heterogeneous palmitoyl-derivatised MAP containing two defined HAV peptide sequences, VP1(11–25) and VP3(102–121), in rabbits immunised with either Freund’s adjuvant or multilamellar liposomes. The immune response was evaluated with a specific enzyme immunoassay using MAP[VP1+VP3], VP1 and VP3 as targets. The avidity of the immune response was measured by a non-competitive enzyme-linked immunosorbent assay and by the surface plasmon resonance technology. Antisera raised against the lipo-MAP peptide entrapped in liposomes demonstrated high avidity of binding with affinity rate constants approximately one order of magnitude greater than those obtained with the Freund’s protocol.
Description8 pages, 5 figures, 4 tables.-- PMID: 12681496 [PubMed].-- Printed version published Apr 10, 2003.-- Edited by Hans-Dieter Klenk.
Publisher version (URL)http://dx.doi.org/10.1016/S0014-5793(03)00249-7
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