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A Plasmodium falciparum antigen gene coding for a 220-kD glutamate-rich protein (GLURP) has been cloned, and the 783 C-terminal amino acids of this protein (GLURP489–1271) have been expressed as a β-galactosidase fusion protein in Escherichia coli. The encoded 783 amino acid residues contain two areas of repeated amino acid sequences. Antibodies against recombinant GLURP489–1271, as well as against a synthetic peptide corresponding to GLURP899–916, and against a synthetic peptide representing the major glutamate rich repeat sequence from the P. falciparum ring erythrocyte surface antigen (Pf155/RESA) (EENV)6 were examined in 423 individuals (age range 30 days-78 years) living in a malaria holoendemic area of Liberia. In the 5–9-year-old age group, subjects with anti-GLURP489–1271 antibody concentrations greater than the mean value of the group had lower parasite densities than those with low antibody concentrations (P = 0.0151). High levels of anti-GLURP899–916 antibodies did not correlate with low parasite densities. However, high levels of anti-(EENV)6 antibodies were associated with significantly lower parasite densities in the 2–4-year-old age group (P = 0.0189). There was no correlation between the anti-GLURP489–1271 and anti-(EENV)6 antibody responses. The data provide indirect evidence for a protective role of antibodies reacting with recombinant GLURP489–1271 as well as with the synthetic peptide (EENV)6 from the Pf155/RESA.
Past two years | Past Year | Past 30 Days | |
---|---|---|---|
Abstract Views | 1701 | 1356 | 580 |
Full Text Views | 19 | 4 | 0 |
PDF Downloads | 14 | 5 | 0 |