Jan 1, 1988

Protein p126: a parasitophorous vacuole antigen associated with the release of Plasmodium falciparum merozoites

Biology of the Cell
P DelplaceB Fortier

Abstract

The p126 protein is synthesized by P. falciparum between the 32nd and the 36th hour of the erythrocytic cycle, and is localized in the parasitophorous vacuole. It is processed when schizonts rupture and the major fragments (50, 47 and 18 kDa), which are released into culture supernatant, have been characterized using monoclonal antibodies. The 47 kDa fragment has been mapped at the N-terminus of the molecule. The portion of the protein p126 gene coding for this fragment contains 3 introns and is characterized by a sequence coding for 6 repeats of 8 aminoacids and by repeats of TCA/T-AGT coding for a polyserine sequence of 37 serines in a row for the FCR-3 strain. The 50 kDa fragment is also found in culture supernatant when merozoites are released from mature schizonts. The incubation of mature schizonts with leupeptin inhibits the release of merozoites and, in this case, a 56 kDa intermediate product is found. In those conditions, merozoites were observed free in the erythrocyte cytoplasm, the membrane of the parasitophorous vacuole being destroyed. The 50 kDa fragment can be obtained from the 56 kDa fragment by treatment with trypsin (a protease inhibited by leupeptin). Our results suggest that the processing of the 56 kDa fr...Continue Reading

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Mentioned in this Paper

Monoclonal Antibodies
Monoclonal antibodies, antineoplastic
Protease Inhibitors [MoA]
Merozoites
Genus Saimiri
ST5 Protein
Antigens, Protozoan
ST5 wt Allele
Endopeptidases
Proteolytic Enzyme

About this Paper

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