| 注册
首页|期刊导航|中国生物防治学报|昆虫表皮蛋白OfCPH-1的液液相分离性质

昆虫表皮蛋白OfCPH-1的液液相分离性质

杜源哲 陈磊 杨青

中国生物防治学报2026,Vol.42Issue(3):582-590,9.
✕
中国生物防治学报2026,Vol.42Issue(3):582-590,9.DOI:10.16409/j.cnki.2095-039x.2026.01.010

昆虫表皮蛋白OfCPH-1的液液相分离性质

The Liquid-Liquid Phase Separation Properties of the Insect Cuticular Protein OfCPH-1

杜源哲 1陈磊 2杨青3

作者信息

  • 1. 中国农业科学院植物保护研究所/植物病虫害综合治理全国重点实验室,北京 100193
  • 2. 中国农业科学院深圳农业基因组研究所/岭南现代农业科学与技术广东省实验室深圳分中心,深圳 518120
  • 3. 中国农业科学院植物保护研究所/植物病虫害综合治理全国重点实验室,北京 100193||中国农业科学院深圳农业基因组研究所/岭南现代农业科学与技术广东省实验室深圳分中心,深圳 518120
  • 折叠

摘要

Abstract

Insect cuticular proteins,as the major extracellular matrix components of the insect cuticle,are highly diverse in type and sequence characteristics.They play crucial roles in the construction and functional regulation of the cuticle structure,contributing significantly to the integrity and diversity of the insect exoskeleton.The Asian corn borer Ostrinia furnacalis is one of the main stem-boring pests of maize and other crops in China,posing a serious threat to food security.Previous studies have identified a highly abundant CPH family cuticular protein,OfCPH-1,in the head capsule of O.furnacalis larvae.OfCPH-1 can bind to chitosan and form liquid-liquid phase separation(LLPS)condensates.This study focuses on the chitin-binding ability and LLPS behavior of OfCPH-1 to explore its potential role in cuticle assembly.Chitin-binding assays demonstrated that OfCPH-1 has strong binding affinity to α-chitin,despite lacking any previously reported canonical chitin-binding domains in its sequence.LLPS assays showed that full-length OfCPH-1 undergoes LLPS at room temperature in response to changes in ionic strength,forming condensates with an average diameter of(571.99±8.67)nm,whereas truncated peptides containing the 18aa motif or AH-rich motif failed to undergo phase separation.The LLPS capability of OfCPH-1 is likely due to the multiple intrinsically disordered regions(IDRs)in its sequence.Fourier-transform infrared spectroscopy(FTIR)analysis further revealed that,upon phase separation,OfCPH-1 undergoes a conformation shift from random coils to β-sheet structures.This study provides new perspective for understanding the biological function of CPH family cuticular proteins and supports the potential development of novel green pesticides by targeting the LLPS behavior of insect cuticular proteins.

关键词

昆虫表皮蛋白/亚洲玉米螟/液液相分离

Key words

insect cuticular protein/Ostrinia furnacalis/liquid-liquid phase separation

分类

农业科技

引用本文复制引用

杜源哲,陈磊,杨青..昆虫表皮蛋白OfCPH-1的液液相分离性质[J].中国生物防治学报,2026,42(3):582-590,9.

基金项目

国家自然科学基金(32200393) (32200393)

中国农业科学院创新工程(CAAS-ZDRW202304) (CAAS-ZDRW202304)

中国生物防治学报

2095-039X

访问量0
|
下载量0
段落导航相关论文