Research articles
ScienceAsia 51 (2026): 1-8 |doi:
10.2306/scienceasia1513-1874.2026.092
A novel silk-like matrix protein family participates in the
formation of shell and pearl in the mussel Hyriopsis cumingii
Zehui Yina,†, Li Yuana,†, Shanqin Qianb,*, Xiaojun Liuc,d,e,*
ABSTRACT: Shell matrix proteins play an important role in mollusk biomineralization. In this study, three cDNA
clones encoding novel matrix proteins were identified from the mantle of Hyriopsis cumingii and named hicsilin family.
The complete sequence analysis of these cDNA fragments showed that they were silk-like proteins, which construct
the organic frameworks with other biomacromolecules. The predicted biomolecular structure consists of two or more
glycine repeat sequences. Gly accounts for more than 50%, Ser and Tyr account for more than 10% of the amino
acid composition. The sum of these three amino acids exceeds 70%. The analysis of tissue expression and in situ
hybridization showed that the proteins were the prismatic and nacreous layer proteins. RNA interference and shell
regeneration experiment confirmed that hicsilin was involved in the formation of prismatic layer and nacreous layer.
Hicsilin was also found to play an important role in calcium carbonate deposits in pearl sacs.
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| a |
Key Laboratory of Freshwater Aquatic Genetic Resources, Shanghai Ocean University, Ministry of Agriculture,
Shanghai 201306 China |
| b |
Taizhou University, Jiangsu 225300 China |
| c |
Department of Biotechnology and Biomedicine, Yangtze Delta Region Institute of Tsinghua University,
Zhejiang 314000 China |
| d |
Taizhou Innovation Center, Yangtze Delta Region Institute of Tsinghua University, Zhejiang 318000 China |
| e |
Zhejiang Provincial Key Laboratory of Applied Enzymology, Yangtze Delta Region Institute of Tsinghua University,
Jiaxing 314006 China |
* Corresponding author, E-mail: qianshanqin@163.com, txliuxj@vip.163.com
Received 0 0000, Accepted 27 May 2025
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