Department of Microbiology, Department of Molecular Science & Technology, Ajou University School of Medicine, Suwon, 443-721, South Korea.
Parasitol Res. 2009 Nov;105(6):1675-81. doi: 10.1007/s00436-009-1610-y. Epub 2009 Sep 16.
Naegleria fowleri, a ubiquitous pathogenic free-living amoeba, is the most virulent species and causes primary amoebic meningoencephalitis in laboratory animals and humans. The parasite secretes various inducing molecules as biological responses, which are thought to be involved in pathophysiological and immunological events during infection. To investigate what molecules of N. fowleri excretory-secretory proteins (ESPs) are related with amoebic pathogenicity, N. fowleri ESPs fractionated by two-dimensional electrophoresis were reacted with N. fowleri infection or immune sera. To identify immunodominant ESPs, six major protein spots were selected and analyzed by N-terminal sequencing. Finally, six proteins, 58, 40, 24, 21, 18, and 16 kDa of molecular weight, were partially cloned and matched with reference proteins as follow: 58 kDa of exendin-3 precursor, 40 kDa of secretory lipase, 24 kDa of cathepsin B-like proteases and cysteine protease, 21 kDa of cathepsin B, 18 kDa of peroxiredoxin, and 16 kDa of thrombin receptor, respectively. These results suggest that N. fowleri ESPs contained important proteins, which may play an important role in the pathogenicity of N. fowleri.
福氏耐格里阿米巴,一种普遍存在的致病性自由生活阿米巴,是最具毒性的物种,可导致实验动物和人类原发性阿米巴脑膜脑炎。寄生虫会分泌各种诱导分子作为生物反应,这些分子被认为参与感染过程中的病理生理和免疫事件。为了研究福氏耐格里阿米巴分泌排泄蛋白(ESP)的哪些分子与阿米巴的致病性有关,用二维电泳分离福氏耐格里阿米巴的 ESP 与福氏耐格里阿米巴感染或免疫血清反应。为了鉴定免疫优势 ESP,选择了六个主要的蛋白质斑点,并通过 N 端测序进行分析。最后,六个蛋白,分子量分别为 58、40、24、21、18 和 16 kDa,部分克隆并与参考蛋白匹配,分别为:58 kDa 的 exendin-3 前体、40 kDa 的分泌脂肪酶、24 kDa 的组织蛋白酶 B 样蛋白酶和半胱氨酸蛋白酶、21 kDa 的组织蛋白酶 B、18 kDa 的过氧化物酶和 16 kDa 的凝血酶受体。这些结果表明,福氏耐格里阿米巴的 ESP 含有重要的蛋白质,可能在福氏耐格里阿米巴的致病性中发挥重要作用。