EXPRESSION AND ANTIGENICITY OF PLASMODIUM-FALCIPARUM MAJOR MEROZOITE SURFACE PROTEIN (MSP1(19)) VARIANTS SECRETED FROM SACCHAROMYCES-CEREVISIAE
EXPRESSION AND ANTIGENICITY OF PLASMODIUM-FALCIPARUM MAJOR MEROZOITE SURFACE PROTEIN (MSP1(19)) VARIANTS SECRETED FROM SACCHAROMYCES-CEREVISIAE
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DOI：
10.1016/0166-6851(94)90064-7
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发表时间：
1994-02-01
影响因子：
1.5
通讯作者：
KUMAR, S
中科院分区：
文献类型：
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作者：
KASLOW, DC;HUI, G;KUMAR, S
恶性疟原虫裂殖子表面蛋白MSP 1（MSP 1（19））的19 kDa羧基末端片段的四种抗原变体在酿酒酵母中表达为组氨酸标记的分泌多肽（rMSP 1（19）s）。rMSP 1（19）的结构分析表明，酵母分泌的rMSP 1（19）蛋白的第一个EGF样结构域中的单个氨基酸变化（E至Q）导致其二硫键依赖性构象的显著变化。用直接ELISA和竞争ELISA对rMSP 1（19）s的抗原性进行了定性和定量分析。数据表明，MSP 1的保守和变体B细胞决定簇（19）以及作为保护性抗体的已知靶标的表位在rMSP 1中真实地重建（19）。使用所描述的表达系统分泌组氨酸标记的rMSP 1（19）s可能是产生针对恶性疟原虫血液阶段的人类疫苗的正确折叠的免疫原的有效且有效的手段。
Four antigenic variants of the 19-kDa carboxy terminal fragment of Plasmodium falciparum merozoite surface protein, MSP1 (MSP1(19)), were expressed in Saccharomyces cerevisiae as a histidine-tagged, secreted polypeptides (rMSP1(19)s). Structural analysis of the rMSP1(19)s indicated that a single amino acid change (E to Q) in the first EGF-like domain of the yeast-secreted rMSP1(19) proteins caused a significant change in their disulfide bond-dependent conformation. The antigenicity of the rMSP1(19)s were qualitatively and quantitatively analyzed by direct and competitive binding ELISAs. The data indicate that conserved and variant B cell determinants of MSP1(19), as well as epitopes that are known targets of protective antibodies, were recreated authentically in the rMSP1(19)s. Secretion of histidine-tagged rMSP1(19)s using the expression system described may be an efficient and effective means of producing a properly folded immunogen for a human vaccine against the blood stages of P. falciparum.