The biosynthesis of the histidine-rich protein of Plasmodium lophurae and the cloning of its gene in Escherichia coli.
Uninucleate trophozoites and schizonts of Plasmodium lophurae were labeled metabolically with [3H]proline. Analysis of labeled parasites indicated that the histidine-rich protein (HRP) was the major polypeptide synthesized by both developmental stages; in trophozoites it represented a larger proportion of total labeled polypeptides. Polyadenylated RNA was prepared from trophozoites and translated in a rabbit reticulocyte lysate system in the presence of [3H]histidine. As compared to the approx. 50 kDa mature protein, in the cell-free system HRP was synthesized as an approx. 58 kDa precursor polypeptide. Size-selected, polyadenylated RNA was used to construct a complementary double-stranded DNA library in pBR322 and plasmids containing HRP sequences were identified by hybridization with a synthetic oligonucleotide probe.
D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics*; D010961:Plasmodium / Q000235:genetics / Q000378:metabolism*; D014176:Protein Biosynthesis; D011506:Proteins / Q000235:genetics; D000099053:Histidine-Rich Glycoprotein
D011506:Proteins; D000099053:Histidine-Rich Glycoprotein