FEBS Letters | |
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 | |
Garcı́a, Mónica1  Haro, Isabel1  Chan, Weng C3  Pérez, Silvia1  Ercilla, Guadalupe2  | |
[1] Departament de Quı́mica de Pèptids i Proteı̈nes, IIQAB-CSIC, Jordi Girona 18–26, 08034 Barcelona, Spain;Servei d’Immunologia, IDIBAPS, Hospital Clı́nic i Provincial, Barcelona, Spain;School of Pharmaceutical Sciences, University of Nottingham, University Park, Nottingham NG7 2RD, UK | |
关键词: Hepatitis A virus; Multiple antigenic peptide; Peptide synthesis; Liposome; Enzyme-linked immunosorbent assay; Surface plasmon resonance; Boc; tert-butoxycarbonyl; DIEA; N; N-diisopropylethylamine; DIPCDI; N; N-diisopropylcarbodiimide; DMF; dimethylformamide; ELISA; enzyme-linked immunosorbent assay; Fmoc; fluoren-9-ylmethoxycarbonyl; HAV; hepatitis A virus; HOBt; N-hydroxybenzotriazole; HPLC; high-performance liquid chromatography; MAP; multiple antigenic peptides; MLV; multilamellar vesicles; MS; mass spectrometry; OD; optical density; RU; resonance units; SPR; surface plasmon resonance; TBTU; 2(1H-benzotriazol-1-yl)-1; 1; 3; 3-tetramethyluronium tetrafluoroborate; TFA; trifluoroacetic acid; TIPS; triisopropylsilane; | |
DOI : 10.1016/S0014-5793(03)00249-7 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
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RO201912020312851ZK.pdf | 192KB | download |