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Proteomic analysis of adult Galeruca daurica (Coleoptera: Chrysomelidae) at different stages during summer diapause
- Source :
- Comparative biochemistry and physiology. Part D, Genomicsproteomics. 29
- Publication Year :
- 2018
-
Abstract
- Galeruca daurica is a new pest causing great losses in the Inner Mongolian grasslands of China. The adults enter obligatory diapause during summer. However, the molecular mechanism of summer diapause remains unknown. We used iTRAQ to conduct proteomic analysis of adult G. daurica at the pre-diapause (PD), diapause (D) and post-diapause (TD) stages during summer diapause. A total of 139 and 118 differentially expressed proteins (DEPs) were detected in D/PD and TD/D comparisons, respectively. Besides a large number of DEPs involved in metabolic process, stress response, cytoskeletal reorganization, and phagosome pathway, many new proteins related to diapause were found in this study, such as encapsulation-relating proteins, odorant binding proteins, chemosensory proteins and ribosomal proteins. KEGG analysis revealed that the phagosome pathway was the only common significantly enriched pathway in both D/PD and TD/D. In addition, juvenile hormone regulation and Ca2+ signaling may play an important role in the regulation of summer diapause in G. daurica. Our proteomic analysis provides a new insight into the mechanism of obligatory summer diapause, and lays a foundation for future molecular level studies.
- Subjects :
- Proteomics
Physiology
Odorant binding
Biology
Diapause
Diapause, Insect
Biochemistry
03 medical and health sciences
Ribosomal protein
Genetics
Animals
Calcium Signaling
KEGG
Molecular Biology
030304 developmental biology
Phagosome
0303 health sciences
030305 genetics & heredity
Cell biology
Coleoptera
Juvenile Hormones
Proteome
Juvenile hormone
Insect Proteins
PEST analysis
Seasons
Subjects
Details
- ISSN :
- 18780407
- Volume :
- 29
- Database :
- OpenAIRE
- Journal :
- Comparative biochemistry and physiology. Part D, Genomicsproteomics
- Accession number :
- edsair.doi.dedup.....8e01d8da721da294a485626187123580