The United States of America As Represented by the Department of Health

The United States of America, As Represented by the Secretary, Department of Health and Human Services

The United States of America As Represented by the Secretary, Department

Thomas E Wellems

Louis H Miller

Kim Lee Sim

David S Peterson

Chetan Chitnis

Xin-Zhuan Su

Russell J Howard

The present invention provides isolated polypeptides useful in the treatment and prevention of malaria caused byor. In particular, the polypeptides are derived from the binding domains of the proteins in the EBL family as well as the sialic acid binding protein (SABP) onmerozoites. The polypeptides may also be derived from the Duffy antigen binding protein (DABP) onmerozoites.

Binding domains from Plasmodium vivax and Plasmodium falciparum erythrocyte binding proteins

The present invention provides isolated polypeptides useful in the treatment and prevention of malaria caused by or . In particular, the polypeptides are derived from the binding domains of the proteins in the EBL family as well as the sialic acid binding protein (SABP) on merozoites. The polypeptides may also be derived from the Duffy antigen binding protein (DABP) on merozoites.

Binding domains from plasmodium vivax and plasmodium falciparum erythrocyte binding proteins

The present invention provides isolated polypeptides useful in the treatment and prevention of malaria caused by Plasmodium falciparum or P. vivax. In particular, the polypeptides are derived from the binding domains of the proteins in the DBL family as well as the sialic acid binding protein (SABP) on P. falciparum merozoites. The polypeptides may also be derived from the Duffy antigen binding protein (DABP) on P. vivax merozoites.

Binding domains from plasmodium vivax and plasmodium falciparum

The present invention provides isolated polypeptides useful in the treatment and prevention of malaria caused by Plasmodium falciparum or P. vivax. In particular, the polypeptides are derived from the binding domains of the proteins in the EBL family as well as the sialic acid binding protein (SABP) on P. falciparum merozoites. The polypeptides may also be derived from the Duffy antigen binding protein (DABP) on P. vivax merozoites.

Binding domains from Plasmodium vivax and Plasmodium falciparum

The invention relates to isolated clones of DNA from Plasmodium falciparum that encode a histidine-rich protein from that organism. The PfHRPII protein is expressed in P. falciparum-infected erythrocytes. The cloned gene segment includes an intron-exon boundary near the amino-terminus of the coding sequence. The PfHRPII protein has a Mr of 60-80 kDa as determined by SDS-PAGE. This is substantially higher than the molecular weight of about 35 kDa as estimated from the predicted amino acid sequence of PfHRPII. The PfHRPII amino acid sequence includes a hydrophobic leader sequence, consistent with secretion of PfHRPII observed in vivo and in vivo. The amino acid sequence of PfHRPII is also characterized by a number of tandem repeats having a high content of histidine, alanine and aspartic acid.

Recombinant DNA clone containing a genomic fragment of PfHRP-II gene

The present invention resides, in part, in cloned DNA fragments encoding a histidine-rich protein of Plasmodium falciparum (PfHRP-II). PfHRP-II is a malarial antigen that is secreted by the parasite into erythrocytes. The protein is characterized by tandem repeats of high histidine, alanine and aspartate content. The protein is found to have high affinity for divalent cations. Cloning and characterization of the PfHRP-II gene are described, as are antibodies against PfHRP-II.

A histidine rich antigen, designated PfHRP-II, has been synthesized from a recombinant DNA clone containing a genomic fragment of Plasmodium falciparum. PfHRP-II is a protein exported from the parasite into the body fluid. This protein passes through the host erythrocyte in concentrated packets and is released from the infected erythrocyte into the body fluid. The antigen has been isolated and is useful for protection against malaria.

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Rockville, MD, United States of America

Thomas E Wellems