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Analysis of antigenicity and immunogenicity of five different chemically defined constructs of a peptide

Authors :
Isabelle Wolowczuk
Hélène Gras-Masse
André Capron
C. Mazingue
Claude Auriault
Marc Bossus
André Tartar
M. Marguerite
Source :
Molecular Immunology. 29:793-800
Publication Year :
1992
Publisher :
Elsevier BV, 1992.

Abstract

The aim of this study was to compare the antigenicity and the immunogenicity of five constructs of a peptide, including the peptide in single copy, a tandem repeat containing three copies, a copolymer with glutaraldehyde and two constructs based on the MAP (Multiple Antigenic Peptide) model, one containing two copies (MAP-2) and the other, eight copies of the peptide (MAP-8). The peptide used in this test was the 115-131 sequence derived from the rSm28-GST antigen of Schistosoma mansoni. All constructs were recognized by rSm28-GST specific antibodies in solid phase immunoassays. However, the binding was higher when the MAP-8 was used as antigen at least partly because of its better coating on the microtiter plates. In vitro lymphoproliferative assays showed that polymer was mitogenic, repeat and MAP-2 did not stimulate rSm28-GST specific T cells while MAP-8 induced a slight response. The injection of MAP-8 to rats led to important antibody and T cell responses higher than those obtained with the other constructs. The IgG2a (cytotoxic antibody in schistosomiasis)/IgG2c (blocking antibody) ratio was independent of the immunogen. Taken together these results demonstrate that both the antigenicity and the immunogenicity of a peptide containing T and B cell epitope(s) are strongly related to the molecular form whereby it is presented and that the MAP-8 construct can be useful in serodiagnosis or in vaccination trials using synthetic peptides.

Details

ISSN :
01615890
Volume :
29
Database :
OpenAIRE
Journal :
Molecular Immunology
Accession number :
edsair.doi.dedup.....fa0c89050d4397071e160dc5f318ec89
Full Text :
https://doi.org/10.1016/0161-5890(92)90189-5