1921
Volume 46, Issue 3
  • ISSN: 0002-9637
  • E-ISSN: 1476-1645
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Abstract

Abstract

A antigen gene coding for a 220-kD glutamate-rich protein (GLURP) has been cloned, and the 783 C-terminal amino acids of this protein (GLURP) have been expressed as a β-galactosidase fusion protein in . The encoded 783 amino acid residues contain two areas of repeated amino acid sequences. Antibodies against recombinant GLURP, as well as against a synthetic peptide corresponding to GLURP, and against a synthetic peptide representing the major glutamate rich repeat sequence from the ring erythrocyte surface antigen (Pf155/RESA) (EENV) 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-GLURP antibody concentrations greater than the mean value of the group had lower parasite densities than those with low antibody concentrations ( = 0.0151). High levels of anti-GLURP antibodies did not correlate with low parasite densities. However, high levels of anti-(EENV) antibodies were associated with significantly lower parasite densities in the 2–4-year-old age group ( = 0.0189). There was no correlation between the anti-GLURP and anti-(EENV) antibody responses. The data provide indirect evidence for a protective role of antibodies reacting with recombinant GLURP as well as with the synthetic peptide (EENV) from the Pf155/RESA.

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/content/journals/10.4269/ajtmh.1992.46.307
1992-03-01
2017-11-23
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