Human antibodies to the polymorphic block 2 domain of the Plasmodium falciparum merozoite surface protein 1 (MSP-1) exhibit a highly skewed, peptide-specific light chain distribution.

Hélène Jouin (1, 2) , Olivier Garraud (3) , Shirley Longacre (2) , Françoise Baleux (4) , Odile Mercereau-Puijalon (2) , Geneviève Milon (5)

1 Schistosomiase, paludisme et inflammation
2 Immunologie moléculaire des parasites
3 GIMAP - Groupe Immunité des Muqueuses et Agents Pathogènes
4 Chimie Organique
5 Immunophysiologie et Parasitisme Intracellulaire

Antibodies to polymorphic block 2 of the Plasmodium falciparum merozoite surface protein 1 (MSP-1) present a paradoxical association with acquired protection against clinical malaria, while showing restricted and fixed specificity, reminiscent of antigenic sin. We report here that these antibodies present a highly imbalanced, peptide-specific light chain distribution. This was not observed with several other parasite-derived peptides or antigens. These data point to a skewed immune response to MSP-1 block 2 that is constrained both in specificity and chain usage. This is the first report of a biased response to polymorphic epitopes of a surface antigen in malaria parasites.

Domaines: Microbiologie et Parasitologie

Hélène Jouin, Olivier Garraud, Shirley Longacre, Françoise Baleux, Odile Mercereau-Puijalon, et al.. Human antibodies to the polymorphic block 2 domain of the Plasmodium falciparum merozoite surface protein 1 (MSP-1) exhibit a highly skewed, peptide-specific light chain distribution.. Immunology and Cell Biology, 2005, 83 (4), pp.392-5. ⟨10.1111/j.1440-1711.2005.01343.x⟩. ⟨pasteur-00166674⟩