MassIVE MSV000098331

Partial Public PXD065473

Proteome-wide analysis and surface protein isolation for secretome characterization reveal insights into the biology of the leaf-cutter ant Acromyrmex echinatior

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Description

The leaf-cutter ant Acromyrmex echinatior secretes a protein layer that covers their exoskeleton and physically interacts with biotic and abiotic factors, including their symbiotic bacteria Pseudonocardia. In this study, in order to characterize both the global proteome and the externally-secreted cuticular protein layer of A. echinatior, we utilize a novel, dual-layered proteomic approach. Using diaPASEF, we quantified 4,428 proteins across four early adult stages, uncovering distinct age-dependent protein clusters enriched in muscle development, lipid metabolism, and immune-related responses. We then developed a novel acid-based extraction method to isolate the externally-secreted protein layer, identifying 323 secreted proteins via ddaPASEF acquisition, many of which were temporally upregulated and associated with various functions such as environmental stress response, microbial defense, and cuticle structural maturation. Notably, tropomyosin-family proteins were both highly enriched in the external-secretome and exhibited significant changes across the early adult timepoints, potentially linking these ion-binding molecules to the metal-enrichment processes that takes place during this crucial stage. [doi:10.25345/C5PG1J17C] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Leaf-cutter ant, secretome, biomineralization ; DatasetType:Proteomics

Contact

Principal Investigators:
(in alphabetical order) 		Lingjun Li, University of Wisconsin-Madison, United States
Submitting User: timohuangtw
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Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

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