Minimal variation in the Pfs28 ookinete antigen from Philippine field isolates of Plasmodium falciparum

• Published in: Molecular and biochemical parasitology Vol. 87; no. 1; pp. 97 - 99
• Main Authors: Hafalla, Julius Clemence R, Santiago, Mario Luis O, Pasay, Ma.Cielo J, Ramirez, Bernadette L, Gozar, Mary Margaret G, Saul, Allan, Kaslow, David C
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.07.1997
• Subjects: 28-kDa sexual stage antigen; Animals; Antigenic Variation - genetics; Antigens, Protozoan - genetics; Antigens, Surface - genetics; DNA, Protozoan - genetics; Epitopes - genetics; Freshwater; Humans; Malaria; Malaria Vaccines; Malaria, Falciparum - parasitology; Molecular Sequence Data; Ookinete; Pfs28; Plasmodium falciparum; Plasmodium falciparum - genetics; Plasmodium falciparum - growth & development; Plasmodium falciparum - immunology; Plasmodium falciparum - isolation & purification; Point Mutation; Protozoan Proteins - genetics; Sequence variation; Transmission blocking vaccine; Philippines; Plasmodium falciparum; 28-kDa sexual stage antigen; MSP1, merozoite Surface Protein 1; Pfs28; Ookinete; Malaria; Sequence variation; EGF, epidermal growth factor; Transmission blocking vaccine; PCR, polymerase chain reaction; EDTA, ethylenediamine tetraacetic acid; Pfs28, Plasmodium falciparum 28-kilodalton zygote/ookinete surface protein
• ISSN: 0166-6851; 1872-9428
• DOI: 10.1016/S0166-6851(97)00042-X

Disrupting the sexual stage of the malaria parasite life cycle is the main goal of transmission-blocking vaccine development. A 28-kilodalton surface antigen, Pfs28, is expressed on the ookinete stage of the human malaria parasite, Plasmodium falciparum, antibodies to which inhibit ookinete development in the mosquito midgut. Homologues of Pfs28 in the avian malaria parasite, P. gallinaceum, and the rodent malarial parasite, P. berghei, confer transmission-blocking immunity experimental malaria parasite infections in their respective hosts. Polymorphism of malaria parasite antigens makes the determination of their amino acid sequence diversity in field isolates prior to vaccine trials a prudent exercise.