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

Author:

Wang Yu‐Jun1ORCID,Liu Qing‐Song2,Liu Li‐Ping3ORCID,Zhang Yi‐Chuan3,Qiu Shuang4,Zhang Wen‐Guang3,Lin Jin‐Hang2,Qin Yu‐Ting3,Wang Xin2ORCID,Wu Yue‐Ying3,Zhao Ping2ORCID,Xia Qing‐You2ORCID,Ding Ling3,Rong Dong‐Ying3,Wang Hong13ORCID,Dong Zhao‐Ming2ORCID

Affiliation:

1. Institute of Sericulture Chengde Medical University Chengde Hebei China

2. Integrative Science Center of Germplasm Creation in Western China (CHONGQING) Science City, Biological Science Research Center Southwest University Chongqing China

3. Guangxi Key Laboratory of Beibu Gulf Marine Biodiversity Conservation, Ocean College Beibu Gulf University Qinzhou China

4. College of Life Science and Technology Huazhong Univeristy of Science and Technology Wuhan Hubei China

Abstract

AbstractCaddisworms (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.

Funder

National Natural Science Foundation of China

Natural Science Foundation of Chongqing Municipality

Publisher

Wiley

Subject

Insect Science,Genetics,Molecular Biology

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