I. Godard et al., ANTIGENICITY AND IMMUNOGENICITY OF P-30-DERIVED PEPTIDES IN EXPERIMENTAL-MODELS OF TOXOPLASMOSIS, Molecular immunology, 31(17), 1994, pp. 1353-1363
P30, also referred to as SAG-1, is now recognized as a major Toxoplasm
a gondii antigen potentially important for both diagnosis and immunopr
ophylaxis of toxoplasmosis. By using predictive algorithms, five synth
etic peptides (48-67, 82-102, 213-230, 238-256 and 279-285) derived fr
om P30, were investigated for B- and T-cell determinants in mouse and
rat experimental models. Antibody recognition appeared more broadly di
stributed along the P30 sequence, whereas T-cell recognition was mainl
y targeted on the 238-256 peptide. In the absence of any carrier prote
in, this peptide induced a B- and T-cell immune response independent o
f the route of immunization (oral route or subcutaneous injection). Th
is peptide (238-256) induced multiple antibody isotypes. In contrast w
ith the 238-256 peptide, the 48-67 peptide, either free or in the form
of a multiple antigenic peptide (MAP) construct or the 279-295 peptid
e, elicited antibodies associated with a TH2 response. This study repo
rts for the first time the analysis of the antigenic and immunogenic p
roperties of P30-derived peptides and are potentially useful for vacci
nal strategies incorporating the P30 Toxoplasma gondii antigen.