Isolation and characterization of two novel serpins from the tick Rhipicephalus haemaphysaloides

文献类型： 外文期刊

第一作者： Yu, Yingfang

作者： Yu, Yingfang;Cao, Jie;Zhou, Yongzhi;Zhang, Honshuang;Zhou, Jinlin

作者机构：

关键词： Rhipicephalus haemaphysaloides;Serpin;Chymotrypsin inhibition;RNA interference

期刊名称：TICKS AND TICK-BORNE DISEASES （ 影响因子：3.744； 五年影响因子：3.693 ）

ISSN： 1877-959X

年卷期： 2013 年 4 卷 4 期

页码：

收录情况： SCI

摘要： Two novel serpins with anti-chymotrypsin activity, RHS-1 and RHS-2, were identified in the tick Rhipicephalus haemaphysaloides. The complementary cDNA sequence of RHS-1 was 1286 base pairs (bp) and encoded a deduced 403-amino acid protein with a signal peptide, whereas that of RHS-2 was 1682 bp and encoded a deduced 380-amino acid protein with no signal peptide. Although both RHS-1 and RHS-2 exhibited high sequence similarities to known serpins from other ticks, the level of similarity at the amino acid level between the 2 serpins characterized here was only 32.5%. Salivary gland-specific expression of RHS-1 and midgut-specific expression of RHS-2 were found by Western blot using the relevant antiserum. We tested the ability of purified recombinant rRHS-1 and rRHS-2 to inhibit various serine proteases and found that both significantly inhibited chymotrypsin (95.6% and 94.2%, respectively). We further demonstrated that RHS-1, but not RHS-2 exhibited anticoagulation activity, based on activated partial thromboplastin time (APTI). Disruption of the genes encoding the 2 serpins with RNA interference (RNAi) led to a significant decrease in tick attachment and engorgement rates. These results indicate that RHS-1 and RHS-2 are 2 hovel serpins with anti-chymotrypsin activity that are involved in blood feeding of R. haemaphysaloides. (C) 2013 Elsevier GmbH. All rights reserved.

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