The silk gland proteome of Stenopsyche angustata provides insights into the underwater silk secretion

IF 2.3 2区 农林科学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
Yu-Jun Wang, Qing-Song Liu, Li-Ping Liu, Yi-Chuan Zhang, Shuang Qiu, Wen-Guang Zhang, Jin-Hang Lin, Yu-Ting Qin, Xin Wang, Yue-Ying Wu, Ping Zhao, Qing-You Xia, Ling Ding, Dong-Ying Rong, Hong Wang, Zhao-Ming Dong
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Abstract

Caddisworms (Trichoptera) spin adhesive silks to construct a variety of underwater composite structures. Many studies have focused on the fibroin heavy chain of caddisworm silk and found that it contains heavy phosphorylation to maintain a stable secondary structure. Besides fibroins, recent studies have also identified some new silk proteins within caddisworm silk. To better understand the silk composition and its secretion process, this study reports the silk gland proteome of a retreat-building caddisworm, Stenopsyche angustata Martynov (Trichoptera, Stenopsychidae). Using liquid chromatography tandem mass spectrometry (LC-MS/MS), 2389 proteins were identified in the silk gland of S. angustata, among which 192 were predicted as secreted silk proteins. Twenty-nine proteins were found to be enriched in the front silk gland, whereas 109 proteins were enriched in the caudal silk gland. The fibroin heavy chain and nine uncharacterized silk proteins were identified as phosphorylated proteins. By analysing the sequence of the fibroin heavy chain, we found that it contains 13 Gly/Thr/Pro-rich regions, 12 Val/Ser/Arg-rich regions and a Gly/Arg/Thr-rich region. Three uncharacterized proteins were identified as sericin-like proteins due to their larger molecular weights, signal peptides and repetitive motifs rich in serine. This study provides valuable information for further clarifying the secretion and adhesion of underwater caddisworm silk.

Abstract Image

angustata的丝腺蛋白质组提供了对水下丝分泌的深入了解。
Caddisworms(毛翅目)通过旋转粘性丝绸来构建各种水下复合结构。许多研究都集中在球童丝的丝素蛋白重链上,发现它含有重磷酸化以维持稳定的二级结构。除了纤维蛋白,最近的研究还发现了球童虫丝中的一些新的丝蛋白。为了更好地了解其丝的组成及其分泌过程,本研究报道了一种撤退建筑球虫Stenopsyche angustata Martynov(毛翅目,Stenopsynchidae)的丝腺蛋白质组。利用液相色谱-质谱联用技术(LC-MS/MS),在扬古斯塔丝腺中鉴定出2389种蛋白质,其中192种为分泌型丝蛋白。29种蛋白质在前部丝腺富集,而109种蛋白质在尾部丝腺富集。丝素蛋白重链和9种未鉴定的丝蛋白被鉴定为磷酸化蛋白。通过对丝素蛋白重链序列的分析,我们发现它包含13个Gly/Thr/Pro富集区、12个Val/Ser/Arg富集区和一个Gly/Arg/Thr富集区。三种未表征的蛋白质由于其较大的分子量、信号肽和富含丝氨酸的重复基序而被鉴定为丝胶样蛋白质。该研究为进一步阐明水下球童丝的分泌和粘附提供了有价值的信息。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Insect Molecular Biology
Insect Molecular Biology 生物-昆虫学
CiteScore
4.80
自引率
3.80%
发文量
68
审稿时长
6-12 weeks
期刊介绍: Insect Molecular Biology has been dedicated to providing researchers with the opportunity to publish high quality original research on topics broadly related to insect molecular biology since 1992. IMB is particularly interested in publishing research in insect genomics/genes and proteomics/proteins. This includes research related to: • insect gene structure • control of gene expression • localisation and function/activity of proteins • interactions of proteins and ligands/substrates • effect of mutations on gene/protein function • evolution of insect genes/genomes, especially where principles relevant to insects in general are established • molecular population genetics where data are used to identify genes (or regions of genomes) involved in specific adaptations • gene mapping using molecular tools • molecular interactions of insects with microorganisms including Wolbachia, symbionts and viruses or other pathogens transmitted by insects Papers can include large data sets e.g.from micro-array or proteomic experiments or analyses of genome sequences done in silico (subject to the data being placed in the context of hypothesis testing).
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