Binding domains from Plasmodium vivax and Plasmodium...

Organic compounds -- part of the class 532-570 series – Organic compounds – Carbohydrates or derivatives

Reexamination Certificate

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Reexamination Certificate

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06962987

ABSTRACT:
The present invention provides isolated polypeptides useful in the treatment and prevention of malaria caused byPlasmodium falciparumorP. 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) onP. falciparummerozoites. The polypeptides may also be derived from the Duffy antigen binding protein (DABP) onP. vivaxmerozoites.

REFERENCES:
patent: 5144007 (1992-09-01), Pfahl
patent: 5198347 (1993-03-01), Miller et al.
patent: 5849306 (1998-12-01), Sim
patent: 5993827 (1999-11-01), Sim
patent: 6392026 (2002-05-01), Sim et al.
patent: WO 93/18160 (1993-09-01), None
Adams, et al., A family of erythrocyte binding proteins of malaria parasites; Proc. Natl. Acad. Sci. USA, vol. 89, pp. 7085-7089; Aug. 1992.
Bamwell, J.W. , et al., In vitro Evaluation of the Role of the duffy Blood Group in Erythrocyte byPlasmodium vivax, J. Exp. Med., 169:1795-1802, May 1989.
Borst, et al., Antigenic Variation in Malaria, Cell 82:1-4, Jul. 14, 1995.
Chitnis, C., et al., Identification of the Erythrocyte Binding Domains . . . J. Exper. Med. 180:497-506, Aug., 1994.
Dalton, J.P., et al., Blocking the receptor-mediated invasion of erythrocytes byPlasmodioum knolesimalaria with sulfated polysaccharides and glycosaminoglyans, Eur. J. Biochem., 195:789-794, 1991.
Fang et al., Cloning of thePlasmodium vivaxDuffy receptor; Mol and Biochem Parasitology; vol. 44(1), pp. 125-132; Jan. 1991.
Haynes, J.D., et al., Receptor-Like Specificity of aPlasmodium knowlesiMalarial Protein the Binds to Duffy Antigen Ligands on Erythrocytges, J. Expl. Med., 167:1873-1881, Jun. 1988.
Holt, E.H., et al., Erythrocyte Invasion by twoPlasmodium falciparumIsolates Differing in Sialic Acid Dependency in the Presence of Glycophorin A Antibodies, Am. J. Trop. Med. Hyg., 40(3): 245-251, Mar. 1989.
Miller, L. H., et al., Identification ofPlasmodium knowlesierythrocyte binding proteins, Molecular and Biochemical Parasitology, 31:217-222, 1988.
Orlandi, P.A., et al., Characterization of the 175-kilodalton erythrocyte binding antigen ofPlasmodium falciparum, Molecular and Biochemical Parasitology, 40:285-294, 1990.
Perkins, M.E., et al., Sialic Acid-Dependent Binding ofPlasmodium falciparumMerozoite Surface Antigen, Pf200, to Human Erythrocytes, J. of Immunology, 141(9):3190-3196, Nov. 1, 1998.
Sim et al., Primary structure of the 175KPlasmodium falciparumErythrocyte binding antigen and identification of a peptide which elicits antibodies that inhibit malaria merozoite invasion; J of Cell Biology, vol. 111, pp. 1877-1884; Nov., 1990.
Sim, et al., Receptor ad Ligand Domains for Invasion of Erythrocytes byPlasmodium falciparum, Science 264:1941-1944, Jun. 24, 1994.
Su, et al., the Large Diverse gene Family var Encodes Proteins Involved in Cytoadherence and Antigenic . . . Cell 82:89-100, Jul. 14, 1985.
Wertheimer, S.P., et al.,Plasmodium vivzxInteraction with the Human Duffy Blood Group glycoprotein: Indentification of a Parasite Receptor-like Protein, Experimental Parasitology, 69:340-350, 1989.

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