原生动物寄生虫病的治疗具有挑战性,因此,识别和分析新药靶标非常重要。寄生虫在宿主生物体内存活,有些需要中间宿主来完成它们的生命周期。改变宿主环境会给寄生虫带来压力,适应通常伴随着大量热休克蛋白(Hsps)的表达。在Hsps中,Hsp90蛋白在应激环境中起重要作用。然而,很少有关于Hsp90蛋白的计算研究来比较分析它们作为潜在的寄生虫药物靶标。这里,试图详细了解主机之间的差异,载体和寄生Hsp90蛋白进行大规模生物信息学分析。总共104个Hsp90序列根据其细胞定位分为三组;即细胞溶质,线粒体和内质网(ER)。Further,寄生虫蛋白根据寄生虫的类型(原生动物,蠕虫和外寄生虫)。一级序列分析,系统发育树计算,Hsp90蛋白的基序分析和理化性质表明,尽管这些蛋白的整体结构保守,寄生Hsp90蛋白具有独特的特征,可以将它们与人类区分开来,因此令人鼓舞的想法,即应该进一步分析原生动物Hsp90蛋白作为潜在的药物靶标。
The treatment of protozoan parasitic diseases is challenging, and thus identification and analysis of new drug targets is important. Parasites survive within host organisms, and some need intermediate hosts to complete their life cycle. Changing host environment puts stress on parasites, and often adaptation is accompanied by the expression of large amounts of heat shock proteins (Hsps). Among Hsps, Hsp90 proteins play an important role in stress environments. Yet, there has been little computational research on Hsp90 proteins to analyze them comparatively as potential parasitic drug targets. Here, an attempt was made to gain detailed insights into the differences between host, vector and parasitic Hsp90 proteins by large-scale bioinformatics analysis. A total of 104 Hsp90 sequences were divided into three groups based on their cellular localizations; namely cytosolic, mitochondrial and endoplasmic reticulum (ER). Further, the parasitic proteins were divided according to the type of parasite (protozoa, helminth and ectoparasite). Primary sequence analysis, phylogenetic tree calculations, motif analysis and physicochemical properties of Hsp90 proteins suggested that despite the overall structural conservation of these proteins, parasitic Hsp90 proteins have unique features which differentiate them from human ones, thus encouraging the idea that protozoan Hsp90 proteins should be further analyzed as potential drug targets.