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Identification of a Conserved Region ofPlasmodium falciparumMSP3 Targeted by Biologically Active Antibodies to Improve Vaccine Design
Author(s) -
Subhash Singh,
Soe Soé,
J. Santiago Mejia,
Christian Roussilhon,
Michael Theisen,
Giampietro Corradin,
Pierre Druilhe
Publication year - 2004
Publication title -
the journal of infectious diseases
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.69
H-Index - 252
eISSN - 1537-6613
pISSN - 0022-1899
DOI - 10.1086/423208
Subject(s) - antigenicity , epitope , antibody , plasmodium falciparum , biology , malaria vaccine , virology , antigen , peptide sequence , malaria , microbiology and biotechnology , immunology , genetics , gene
Merozoite surface protein 3 (MSP3) is a target of antibody-dependent cellular inhibition (ADCI), a protective mechanism against Plasmodium falciparum malaria. From the C-terminal half of the molecule, 6 overlapping peptides were chosen to characterize human immune responses. Each peptide defined at least 1 non-cross-reactive B cell epitope. Distinct patterns of antibody responses, by level and IgG subclass distribution, were observed in inhabitants of a malaria-endemic area. Antibodies affinity purified toward each peptide differed in their functional capacity to mediate parasite killing in ADCI assays: 3 of 6 overlapping peptides had a major inhibitory effect on parasite growth. This result was confirmed by the passive transfer of anti-MSP3 antibodies in vivo in a P. falciparum mouse model. T helper cell epitopes were identified in each peptide. Antigenicity and functional assays identified a 70-amino acid conserved domain of MSP3 as a target of biologically active antibodies to be included in future vaccine constructs based on MSP3.

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