Dual roles of salivary proteins in feeding and silk fiber coating in the spider mite Tetranychus urticae

The two-spotted spider mite (Tetranychus urticae), a plant cell-sucking herbivore, produces nanoscale adhesive silk fibers. Previous silk proteomics identifies Fibroin-1 and Fibroin-2, differing from 17 silk proteins predicted by genome sequencing. Here we demonstrate that these candidate fibroins, along with sFibroin-1 (highly similar to Fibroin-1), function as salivary proteins rather than silk proteins. The three candidate fibroins are expressed in salivary glands, which lack direct connection to silk glands. Fluid beads-on-a-string patterns on silk fibers and fluid patches at feeding sites, likely saliva, are observed. Consistent with this, silk proteomics detects the eight predicted silk proteins and 66 salivary proteins including the three candidate fibroins. RNAi of Fibroin-1 and sFibroin-1 decreases feeding duration, survival, and fecundity, while RNAi of Fibroin-2 reduces silk fiber thickness. The results suggest that Fibroin-1 and sFibroin-1 are involved during feeding, while Fibroin-2 provides adhesive coating to silk fibers, demonstrating saliva's dual role in this species.

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Publication Details

Journal
Communications Biology
Published
2025-10-17
DOI
https://doi.org/10.1038/s42003-025-08885-0
Citations
5
Primary Topic
Silk-based biomaterials and applications
Type
article
Field-Weighted Citation Impact
2.99

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article

Dual roles of salivary proteins in feeding and silk fiber coating in the spider mite Tetranychus urticae

Naoki Takeda, Hisashi Murakami, Dagmar Voigt, Yuka Arai et al.
5 citations
Communications Biology
Silk-based biomaterials and applications
2.99
article

Dual roles of salivary proteins in feeding and silk fiber coating in the spider mite Tetranychus urticae

Naoki Takeda, Hisashi Murakami, Dagmar Voigt, Yuka Arai, Takeshi Suzuki, Shinya Komoto
article en
5 citations

Abstract

The two-spotted spider mite (Tetranychus urticae), a plant cell-sucking herbivore, produces nanoscale adhesive silk fibers. Previous silk proteomics identifies Fibroin-1 and Fibroin-2, differing from 17 silk proteins predicted by genome sequencing. Here we demonstrate that these candidate fibroins, along with sFibroin-1 (highly similar to Fibroin-1), function as salivary proteins rather than silk proteins. The three candidate fibroins are expressed in salivary glands, which lack direct connection to silk glands. Fluid beads-on-a-string patterns on silk fibers and fluid patches at feeding sites, likely saliva, are observed. Consistent with this, silk proteomics detects the eight predicted silk proteins and 66 salivary proteins including the three candidate fibroins. RNAi of Fibroin-1 and sFibroin-1 decreases feeding duration, survival, and fecundity, while RNAi of Fibroin-2 reduces silk fiber thickness. The results suggest that Fibroin-1 and sFibroin-1 are involved during feeding, while Fibroin-2 provides adhesive coating to silk fibers, demonstrating saliva's dual role in this species.

Communications BiologyVol. 8(1)
Okinawa Institute of Science and Technology Graduate University (JP), Technische Universität Dresden (DE), Tokyo University of Agriculture and Technology (JP)
Keio University, Cabinet Office, Government of Japan, Technische Universität Dresden, Tokyo University of Agriculture, Tokyo University of Agriculture and Technology, Japan Society for the Promotion of Science, Bio-oriented Technology Research Advancement Institution, National Institute for Basic Biology, Moonshot Research and Development Program
Openalex Percentile: Top 9%
Silk-based biomaterials and applications
2.99
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