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Identification of a New Peritrophic Membrane Protein from Larval Holotrichia parallela (Coleoptera: Motschulsky)

机译:鉴定了一种新的来自幼虫Holotrichia parallela(鞘翅目:Motschulsky)的营养蛋白

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摘要

Peritrophic membranes (PMs) are composed of proteins, proteoglycans and chitin that play important roles in the structural formation and function of the PM. This study identified and characterized a new chitin binding protein named HpCBP45 by immunoscreening of the Holotrichia parallela larvae midgut expression library. The predicted amino acid sequence indicates that it contains eight tandem chitin binding domains belonging to the peritrophin-A family. The HpCBP45 protein was expressed as a recombinant protein in the yeast Pichia pastoris and chitin binding assay demonstrated that recombinant HpCBP45 protein could strongly bind to chitin. qRT-PCR analysis showed that HpCBP45 was mainly localized in the midgut, further confirming the H. parallela PM belongs to Type I PM. The discovery and characterization of the peritrophic membrane protein HpCBP45 provides a basis for the further investigation of its biochemical and physiological functions in H. parallela.
机译:养分膜(PMs)由蛋白质,蛋白聚糖和几丁质组成,它们在PM的结构形成和功能中起重要作用。这项研究通过免疫筛选平行小花parallel幼虫中肠表达文库,鉴定并鉴定了一种新的几丁质结合蛋白HpCBP45。预测的氨基酸序列表明它含有八个串联的几丁质几丁质结合域,属于peritrophin-A家族。 HpCBP45蛋白在酵母毕赤酵母中表达为重组蛋白,几丁质结合试验表明重组HpCBP45蛋白可以与几丁质牢固结合。 qRT-PCR分析表明,HpCBP45主要定位于中肠,进一步证实了H.parallela PM属于I型PM。营养膜蛋白HpCBP45的发现和表征为进一步研究其在平行虫中的生化和生理功能提供了基础。

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