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A New Type I Peritrophic Membrane Protein from Larval Holotrichia oblita (Coleoptera: Melolonthidae) Binds to Chitin

文献类型： 外文期刊

作者： Liu, Xiaomin 1 ; Li, Jie 4 ; Guo, Wei 2 ; Li, Ruijun 3 ; Zhao, Dan 3 ; Li, Xinna 3 ;

作者机构： 1.Hebei Acad Agr & Forestry Sci, Inst Cereal & Oil Crops, Shijiazhuang 050035, Hebei, Peoples R China

2.China Agr Univ, Plant Sci & Technol Coll, Beijing 102206, Peoples R China

3.Agr Univ Hebei, Biol Control Ctr Plant Pathogens & Plant Pests He, Coll Plant Protect, Baoding 071001, Hebei, Peoples R China

4.Shijiazhuang Dev & Reform Commiss, Shijiazhuang 050011, Hebei, Peoples R China

关键词： peritrophic membrane;Holotrichia oblita;cDNA expression library;chitin binding protein;HoCBP76

期刊名称：INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES （ 影响因子：5.923； 五年影响因子：6.132 ）

ISSN： 1422-0067

年卷期： 2014 年 15 卷 4 期

页码：

收录情况： SCI

摘要： Peritrophic membranes (PMs) are composed of chitin and protein. Chitin and protein play important roles in the structural formation and function of the PM. A new type I PM protein, HoCBP76, was identified from the Holotrichia oblita. HoCBP76 was shown as a 62.3 kDa protein by SDS-PAGE analysis and appeard to be associated with the PM throughout its entire length. In H. oblita larvae, the midgut is the only tissue where HoCBP76 could be detected during the feeding period of the larvae. The predicted amino acid sequence indicates that it contains seven tandem chitin binding domains belonging to the peritrophin-A family. HoCBP76 has chitin binding activity and is strongly associated with the PM. The HoCBP76 was not a mucin-like glycoprotein, and the consensus of conserved cysteines appeared to be CX13-17CX5CX9CX12CX7C. Western blot analysis showed that the abundance of HoCBP76 in the anterior, middle and posterior regions of the midgut was similar, indicating that HoCBP76 was secreted by the whole midgut epithelium, and confirmed the H. oblita PM belonged to the Type I PM. Immunolocalization analysis showed that HoCBP76 was mainly localized in the PM. The HoCBP76 is the first PM protein found in the H. oblita; however, its biochemical and physiological functions require further investigation.

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