Stafford W H, Günder B, Harris A, Heidrich H G, Holder A A, Blackman M J
Division of Parasitology, National Institute for Medical Research, London, UK.
Mol Biochem Parasitol. 1996 Oct 1;80(2):159-69. doi: 10.1016/0166-6851(96)02696-5.
The Plasmodium falciparum merozoite surface protein-1 (MSP-1) is synthesized as a precursor of approximately 195 kDa and is processed to form a complex of polypeptides on the surface of free merozoites. As a result of a second processing event, the entire MSP-1 complex is shed from the surface, apart from a C-terminal fragment that remains anchored to the merozoite membrane. We have identified a 22 kDa protein (p22) on the surface of merozoites by cell surface radioiodination and indirect immunofluorescence assay on unfixed free merozoites. p22 is also a component of the shed MSP-1 complex where it is present in part as a 19 kDa form (p22(19)) as shown by immunochemical and peptide mapping analyses. The soluble complex contains MSP-1-derived polypeptides and p22 in approximately stoichiometrically equal amounts. N-terminal amino acid sequence analyses of p22/p22(19) showed that the protein is not derived from the MSP-1 precursor.
恶性疟原虫裂殖子表面蛋白-1（MSP-1）最初合成时是一种约195 kDa的前体，在游离裂殖子表面加工形成多肽复合物。经过第二次加工后，整个MSP-1复合物从表面脱落，仅留下一个C端片段仍锚定在裂殖子膜上。我们通过细胞表面放射性碘化以及对未固定的游离裂殖子进行间接免疫荧光测定，在裂殖子表面鉴定出一种22 kDa的蛋白（p22）。免疫化学和肽图谱分析表明，p22也是脱落的MSP-1复合物的一个组分，部分以19 kDa的形式（p22(19)）存在。可溶性复合物中MSP-1衍生的多肽和p22的含量大致化学计量相等。对p22/p22(19)的N端氨基酸序列分析表明，该蛋白并非来源于MSP-1前体。
