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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
Author(s) -
Haro Isabel,
Pérez Silvia,
Garcı́a Mónica,
Chan Weng C,
Ercilla Guadalupe
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00249-7
Subject(s) - avidity , liposome , peptide , antigen , immune system , adjuvant , capsid , chemistry , virology , immunoassay , virus , antibody , surface plasmon resonance , antiserum , microbiology and biotechnology , biology , biochemistry , immunology , materials science , nanoparticle , nanotechnology
Multiple 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.