Jongwutiwes S, Tanabe K, Kanbara H
Department of Protozoology, Nagasaki University, Japan.
Mol Biochem Parasitol. 1993 May;59(1):95-100. doi: 10.1016/0166-6851(93)90010-u.
The C-terminal part of the precursor to the major merozoite surface proteins (MSP1) of Plasmodium falciparum contains potential protective epitopes and two cleavage sites for processing which take place prior to erythrocyte invasion by the merozoite. Since sequences available to date are limited and derived from cultured parasites, we have examined the extent of variations of this important part of the MSP1 gene from natural populations. Our sequence analyses of 1.6-1.7 kb from blocks 13-17 of the gene obtained from 19 Thai wild isolates have identified a deletion of a codon and 18 nucleotide substitutions, all of which are dimorphic substitutions and all but one create amino acid exchanges. However, residues at two cleavage sites for the C-terminus 42 kDa polypeptide and the 19-kDa polypeptide, a subfragment of the former, are conserved. Furthermore, all 12 cysteine residues at the C-terminal 19-kDa polypeptide are perfectly conserved, allowing the formation of 2 epidermal growth factor-like structures. These results indicate that in contrast to extensive variations at the N-terminal part of MSP1, limited variations occur at the C-terminal part.
恶性疟原虫主要裂殖子表面蛋白(MSP1)前体的C末端部分包含潜在的保护性表位以及两个加工切割位点,这些切割发生在裂殖子侵入红细胞之前。由于目前可获得的序列有限且来自培养的寄生虫,我们研究了来自自然种群的MSP1基因这一重要部分的变异程度。我们对从19个泰国野生分离株获得的该基因第13 - 17区段的1.6 - 1.7 kb进行序列分析,确定了一个密码子缺失和18个核苷酸替换,所有这些都是双态替换,除一个外其余均导致氨基酸交换。然而,C末端42 kDa多肽和前者的一个亚片段19 kDa多肽的两个切割位点处的残基是保守的。此外,C末端含19 kDa多肽的所有12个半胱氨酸残基完全保守,可形成2个表皮生长因子样结构。这些结果表明,与MSP1 N末端部分的广泛变异相反,C末端部分的变异有限。