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Infection and Immunity, September 1998, p. 4203-4207, Vol. 66, No. 9
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Identification of an Erythrocyte Binding Peptide from the Erythrocyte Binding Antigen, EBA-175, Which Blocks Parasite Multiplication and Induces Peptide-Blocking Antibodies

P. H. Jakobsen,1,* P. M. H. Heegaard,2 C. Koch,3 K. Wasniowska,4 M. M. Lemnge,5 J. B. Jensen,6 and B. K. L. Sim4

Centre for Medical Parasitology, Department of Infectious Diseases, State University Hospital (Rigshospitalet) and Institute of Medical Microbiology and Immunology,1 and Danish Veterinary Laboratory and Protein Laboratory,2 University of Copenhagen, and Section of Immunology, Statens Seruminstitut,3 Copenhagen, Denmark; EntreMed, Medical Center Drive, Rockville, Maryland4; National Institute for Medical Research, Amani Centre, Amani, Tanzania5; and Department of Microbiology, Ezra Taft Institute, Brigham Young University, Provo, Utah6

Received 26 November 1997/Returned for modification 25 February 1998/Accepted 3 June 1998

A biotinylated peptide covering a sequence of 21 amino acids (aa) from the erythrocyte binding antigen (EBA-175) of Plasmodium falciparum bound to human glycophorin A, an erythrocyte receptor for merozoites, as demonstrated by enzyme-linked immunosorbent assay (ELISA) and to erythrocytes as demonstrated by flow cytometry analysis. The peptide, EBA(aa1076-96), also bound to desialylated glycophorin A and glycophorin B when tested by ELISA. The peptide blocked parasite multiplication in vitro. The glycophorin A binding sequence was further delineated to a 12-aa sequence, EBA(aa1085-96), by testing the binding of a range of truncated peptides to immobilized glycophorin A. Our data indicate that EBA(aa1085-96) is part of a ligand on the merozoite for binding to erythrocyte receptors. This binding suggests that the EBA(aa1085-96) peptide is involved in a second binding step, independent of sialic acid. Antibody recognition of this peptide sequence may protect against merozoite invasion, but only a small proportion of sera from adults from different areas of malaria transmission showed antibody reactivities to the EBA(aa1076-96) peptide, indicating that this sequence is only weakly immunogenic during P. falciparum infections in humans. However, Tanzanian children with acute clinical malaria showed high immunoglobulin G reactivity to the EBA(aa1076-96) peptide compared to children with asymptomatic P. falciparum infections. The EBA(aa1076-96) peptide sequence from EBA-175 induced antibody formation in mice after conjugation of the peptide with purified protein derivative. These murine sera inhibited EBA(aa1076-96) peptide binding to glycophorin A.

* Corresponding author. Mailing address: Department of Infectious Diseases M7722, Copenhagen University Hospital (Rigshospitalet), Tagensvej 20, DK-2200 Copenhagen N, Denmark. Phone: 45 35 45 74 49. Fax: 45 35 45 68 31. E-mail: pallehoy{at}inet.uni-c.dk.

Infection and Immunity, September 1998, p. 4203-4207, Vol. 66, No. 9
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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