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A member of the HSP90 family from ovine Babesia in China: molecular characterization, phylogenetic analysis and antigenicity

机译：中国绵羊巴贝虫病HSP90家族成员：分子表征，系统发育分析和抗原性

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摘要

Heat shock protein 90 (HSP90) is a key component of the molecular chaperone complex essential for activating many signalling proteins involved in the development and progression of pathogenic cellular transformation. A Hsp90 gene (BQHsp90) was cloned and characterized from Babesia sp. BQ1 (Lintan), an ovine Babesia isolate belonging to Babesia motasi-like group, by screening a cDNA expression library and performing rapid amplification of cDNA ends. The full-length cDNA of BQHsp90 is 2399 bp with an open reading frame of 2154 bp encoding a predicted 83 kDa polypeptide with 717 amino acid residues. It shows significant homology and similar structural characteristics to Hsp90 of other apicomplex organisms. Phylogenetic analysis, based on the HSP90 amino acid sequences, showed that the Babesia genus is clearly separated from other apicomplexa genera. Five Chinese ovine Babesia isolates were divided into 2 phylogenetic clusters, namely Babesia sp. Xinjiang (previously designated a new species) cluster and B. motasi-like cluster which could be further divided into 2 subclusters (Babesia sp. BQ1 (Lintan)/Babesia sp. Tianzhu and Babesia sp. BQ1 (Ningxian)/Babesia sp. Hebei). Finally, the antigenicity of rBQHSP90 protein from prokaryotic expression was also evaluated using western blot and enzyme-linked immunosorbent assay (ELISA).
机译：热休克蛋白90（HSP90）是分子伴侣复合物的关键成分，对于激活许多与病原性细胞转化的发生和发展有关的信号蛋白至关重要。 Hsp90基因（BQHsp90）被克隆并从巴贝斯虫中鉴定。通过筛选cDNA表达文库并快速扩增cDNA末端，将BQ1（Lintan），一种隶属于巴贝斯motasi-like组的绵羊巴贝斯分离株。 BQHsp90的全长cDNA为2399 bp，开放阅读框为2154 bp，编码具有717个氨基酸残基的预测的83 kDa多肽。它显示出与其他apicomplex生物体的Hsp90显着的同源性和相似的结构特征。基于HSP90氨基酸序列的系统发育分析表明，巴贝虫属明显与其他apiplexplexa属分开。将五种中国绵羊巴贝虫分离株分为两个系统发育簇，即巴贝虫。新疆（先前指定为新物种）集群和B. motasi集群可以进一步分为两个亚群（Babesia sp。BQ1（Lintan）/巴贝斯虫sp。Tianzhu和Babesia sp。BQ1（Ningxian）/ Babesia sp。河北） ）。最后，还使用蛋白质印迹和酶联免疫吸附测定（ELISA）评估了原核表达中rBQHSP90蛋白的抗原性。

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