PXD059809-1
PXD059809 is an original dataset announced via ProteomeXchange.
Dataset Summary
| Title | Saliva and silk proteins in spider mites: dual roles in feeding and silk fiber coating |
| Description | Spider mites are leaf cell-sucking herbivores that spin nanoscale silk fibers released from their second mouthpart appendages. Previous studies computationally predicted 17 silk protein genes by whole genome sequencing in the two-spotted spider mite, Tetranychus urticae, while two novel candidates, Fibroin-1 and Fibroin-2, were detected in the silk proteome. In addition, Fibroin-1, sFibroin-1 (high sequence similarity to Fibroin-1), and Fibroin-2 proteins were also detected in the saliva proteome. We investigated whether these three proteins function as silk, saliva, or both. The mRNA for Fibroin-1, sFibroin-1, and Fibroin-2 were all expressed in the salivary glands. Micro-CT scanning confirmed no direct connection between salivary glands and silk glands, i.e., saliva and silk meet each other during simultaneous secretion and spinning. Silk proteomics performed in the present study detected proteins encoded by 8 of the 17 originally predicted genes, as well as Fibroin-1, sFibroin-1, and Fibroin-2 proteins. In addition, cryo-SEM imaging visualized a bead-on-a-string pattern formed by a fluid on the silk fiber, as well as a fluid patch that remains at the piercing site on the leaf surface after mite feeding. Furthermore, RNAi-mediated silencing of Fibroin-1 and sFibroin-1 reduced the feeding duration of mites, resulting in low survival and fecundity. Fibroin-2 RNAi reduced the thickness of single filaments of silk fibers. These results suggest that Fibroin-1, sFibroin-1, and Fibroin-2 proteins are secreted from the salivary glands and then adhere to silk fibers. Fibroin-1 and sFibroin-1 proteins support mites establishing a stable piercing site by adhering the tip of the mouthparts to the leaf surface to suck leaf cell contents with their stylets, while Fibroin-2 coats silk fibers. Eight originally predicted genes are still candidates for silk protein genes. This study revealed the two roles of saliva in leaf cell-sucking herbivorous mites, which include stabilizing mouthparts during feeding and coating silk fibers, providing them with adhesive properties. |
| HostingRepository | jPOST |
| AnnounceDate | 2025-08-27 |
| AnnouncementXML | Submission_2025-08-26_08:00:04.639.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Non peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Yuka Arai |
| SpeciesList | scientific name: cellular organisms; NCBI TaxID: 131567; |
| ModificationList | S-carboxamidomethyl-L-cysteine; L-methionine sulfoxide; residues isobaric at 113.084064 Da; N6-acetyl-L-lysine; Met-loss; Met-loss+Acetyl |
| Instrument | instrument |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
|---|---|---|---|
| 0 | 2025-01-14 23:30:57 | ID requested | |
| ⏵ 1 | 2025-08-26 08:00:05 | announced |
Publication List
| Dataset with its publication pending |
Keyword List
| submitter keyword: acari, spider mites, silk, fibroin, RNAi |
Contact List
| Takeshi Suzuki | |
|---|---|
| lab head | |
| Yuka Arai | |
| contact affiliation | Tokyo university of agriculture and technology |
| dataset submitter | |
Full Dataset Link List
| jPOST dataset URI |
| Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.jpostdb.org/JPST003501/ |




