Molecular cloning of the 82-kDa heat shock protein (HSP90) of Toxoplasma gondii associated with the entry into and growth in host cells
Molecular cloning of the 82-kDa heat shock protein (HSP90) of Toxoplasma gondii associated with the entry into and growth in host cells
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DOI：
10.1016/j.bbrc.2003.10.045
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发表时间：
2003-11-21
影响因子：
3.1
通讯作者：
Nam, HW
中科院分区：
文献类型：
--
作者：
Ahn, HJ;Kim, S;Nam, HW
在抗弓形虫的单抗中，Tg485单抗与一个82 kDa的速殖子胞质蛋白发生特异性反应。该蛋白由胞外速殖子分泌，但在入侵后不释放到寄生虫的液泡中。用Tg485筛选弓形虫表达文库，获得编码该蛋白的cDNA片段。用5‘-RACE方法扩增出全长cDNA并测序。与Tg485反应的82 kDa蛋白的推导氨基酸序列显示，该多肽由708个氨基酸组成，与其他生物的热休克蛋白90(HSP90)家族有显著的同源性，特别是与apicplexan物种的同源性更高。用已知的干扰HSP90功能的药物格尔达那霉素处理后，细胞外速殖子分泌TgHSP90的能力没有受到影响，但速殖子进入宿主细胞的过程和寄生虫在细胞内的生长明显受到干扰。(C)2003 Elsevier Inc.保留所有权利。
Among the monoclonal antibodies (mAb) against Toxoplasma gondii, mAb Tg485 specifically reacted with an 82-kDa cytoplasmic protein of tachyzoites. The protein was secreted from extracellular tachyzoites, but was not released into the parasitophorous vacuole after invasion. The cDNA fragment encoding the protein was obtained by screening a T gondii cDNA expression library with Tg485. The full-length cDNA was amplified by the 5'-RACE method and sequenced. The deduced amino acid sequence of the 82 kDa protein reacting with Tg485 revealed a polypeptide of 708 amino acids showing significant homology to the heat shock protein 90 (HSP90) family of other organisms, especially to those of apicomplexan species. Treatment with geldanamycin, a drug known to interfere with HSP90 function, did not affect the secretion of TgHSP90 from extracellular tachyzoites, but the entry of the tachyzoites into host cells and the intracellular growth of the parasite were significantly disturbed. (C) 2003 Elsevier Inc. All rights reserved.