ArticleScientific reports2017
From EST to novel spider silk gene identification for production of spidroin-based biomaterials.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Post-translational modifications of silk proteins.RSC chemical biology · 2026Review
- Intrinsically disordered linkers and terminal domains codrive aciniform spidroin self-assembly through liquid-liquid phase separation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Critical role of minor eggcase silk component in promoting spidroin chain alignment and strong fiber formation.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
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Authors and funding
10 authors.
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Abstract
A cDNA library from a pool of all the seven silk glands from a tropical spider species was constructed. More than 1000 expressed sequence tag (EST) clones were created. Almost 65% of the EST clones were identified and around 50% were annotated. The cellular and functional distribution of the EST clones indicated high protein synthesis activity in spider silk glands. Novel clones with repetitive amino acid sequences, which is one of the most important characteristics of spider silk genes, were isolated. One of these clones, namely TuSp2 in current research, contains two almost identical fragments with one short C-terminal domain. Reverse transcription (RT) PCR and expression analysis showed that it is expressed in the tubuliform gland and involved in eggcase silk formation. Furthermore, its single repetitive domain can be induced to form various types of materials, including macroscopic fibers, transparent film and translucent hydrogel. This study implies promising potentials for future identification of novel spidroins and development of new spidroin-based biomaterials.
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