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Isolation and partial structural characterization of new Kunitz-type trypsin inhibitors from the pike cestode Triaenophorus nodulosus.
Molecular and Biochemical Parasitology ( IF 1.5 ) Pub Date : 2019-08-24 , DOI: 10.1016/j.molbiopara.2019.111217
Eugene A Rogozhin 1 , Mikhail M Solovyev 2 , Tatiana V Frolova 3 , Galina I Izvekova 3
Affiliation  

The inhibitors produced by the parasitic worms successfully protect them from the host’s proteases and are supposed to underlie the host-parasite specificity. Our previous study has shown that the extracts from the pike tapeworm Triaenophorus nodulosus inhibit host proteinases and commercial trypsin. We aimed to isolate and identify the components responsible for trypsin inactivation. After a two-step separation the molecular masses were measured by SE-HPLC. The sample proved to contain four fractions represented by polypeptides (1–45 kDa) and low-molecular hydrophobic compounds. According to SDS-PAGE analysis, the major polypeptides in the fractions displaying the highest inhibition had masses of 14.4 kDa. The study culminated in partial N-terminal amino acid sequence analysis with a further search for homology. The research revealed two novel Kunitz-type proteins potentially responsible for the inhibitory capacity of the tapeworms against trypsin. Our findings extend the list of cestodes relying on Kunitz-type proteins in the host-parasite molecular cross-talk.



中文翻译:

派克三头草Triaenophorus nodulosus的新型Kunitz型胰蛋白酶抑制剂的分离和部分结构表征。

寄生蠕虫产生的抑制剂成功地保护了它们免受宿主蛋白酶的侵害,并被认为是宿主寄生虫特异性的基础。我们以前的研究表明,派克tape虫Triaenophorus nodulosus的提取物抑制宿主蛋白酶和商业胰蛋白酶。我们旨在分离和鉴定负责胰蛋白酶失活的成分。两步分离后,通过SE-HPLC测量分子量。样品被证明含有多肽(1-45 kDa)和低分子疏水化合物代表的四个部分。根据SDS-PAGE分析,显示出最高抑制作用的部分中的主要多肽的质量为14.4kDa。该研究最终以部分N末端氨基酸序列分析为基础,并进一步寻找同源性。研究发现了两种新型的库尼兹型蛋白,它们可能是蠕虫对胰蛋白酶的抑制能力。我们的研究结果扩展了依赖寄主-寄生虫分子串扰的Kunitz型蛋白质的of类的清单。

更新日期:2019-08-24
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