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

被引:6
|
作者
Zhao, Dan [1 ,2 ]
Guo, Wei [1 ,2 ]
Li, Shaoya [2 ]
Li, Ruijun [2 ]
Xu, Daqing [3 ]
Lu, Xiujun [2 ]
机构
[1] China Agr Univ, Plant Sci & Technol Coll, Beijing 102206, Peoples R China
[2] Agr Univ Hebei, Coll Plant Protect, Baoding 071001, Peoples R China
[3] Agr Univ Hebei, Coll Life Sci, Baoding 071001, Peoples R China
基金
中国国家自然科学基金;
关键词
peritrophic membrane; Holotrichia parallela; midgut; chitin binding protein; HpCBP45; CHITIN-BINDING PROTEINS; MOLECULAR-CLONING; INTESTINAL MUCIN; TRICHOPLUSIA-NI; MATRIX; INSECTS; CDNA; GUT;
D O I
10.3390/molecules191117799
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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.
引用
收藏
页码:17799 / 17809
页数:11
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