Molecular adaptations of Helicoverpa armigera midgut tissue under pyrethroid insecticide stress characterized by differential proteome analysis and enzyme activity assays

Date

2013-06-01

Author

Konus, Metin
Koy, Cornelia
Mikkat, Stefan
Kreutzer, Michael
Zimmermann, Ralf
İşcan, Mesude
Glocker, Michael O.

Metadata

Show full item record

This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Item Usage Stats

70
views

0
downloads

Helicoverpa armigera is an insect that causes important economic losses in crops. To reduce this loss, pyrethroids have been commonly used against H. armigera in farming areas. However, excess and continuous usage of pyrethroids cause resistance in H. armigera. Therefore, expressions of midgut proteins of two H. armigera field populations were compared to those of a susceptible strain by 2-D PAGE and MALDI-ToF-MS. Our results indicate that H. armigera reacts to pyrethroid-induced stress mainly by increasing the expression of energy metabolism-related proteins, such as ATP synthase and arginine kinase. NADPH cytochrome P450 reductase, also up-regulated, could play a role in detoxification of toxic pyrethroid metabolites, such as 3-phenoxybenzaldehyde. Interestingly, while GSTs were not found up-regulated in the comparative proteome analysis, biochemical assays showed significant increases of enzyme activities in both field populations as compared to the susceptible strain. Similarly, although esterases were not found differentially expressed, biochemical assays showed significant increases of esterase activities in both field populations. Thus, esterases are also proposed to be involved in metabolic responses towards pyrethroid insecticide-induced stress. In conclusion, we suggest increased energy metabolism in the midgut tissue of H. armigera as a general prerequisite for compensating the costs of energy-consuming detoxification processes.

Subject Keywords

Genetics, Biochemistry, Physiology, Molecular Biology

URI

https://hdl.handle.net/11511/56912

Journal

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY D-GENOMICS & PROTEOMICS

DOI

https://doi.org/10.1016/j.cbd.2013.04.001

Collections

Department of Biology, Article

Suggestions

OpenMETU
Core

Studies on the mechanism of resistance against pyrethroids in helicoperva armigera : molecular and proteomic approach Konuş, Metin; İşcan, Mesude; Department of Biochemistry (2012) Helicoverpa armigera is an insect, causes important economical losses in crops. To reduce this loss, chemical insecticides such as pyrethroids have been commonly used against H. armigera in farming areas all over the world. However, excess and continuous usages of them cause resistance development in H. armigera. Insects develop resistance against applied insecticides by following three main mechanisms; by reducing the amount of insecticide entering into the insect body, developing insensitivity of the inse...
Genetic diversity of scald (rhynchosporium secalis) disease resistant and sensitive Turkish barley seed sources as determined with simple sequence repeats Dizkırıcı, Ayten; Kaya, Zeki; Department of Biology (2006) Scald disease (Rhynchosporium secalis) is one of the major plant diseases causing considerable yield loss in barley (Hordeum vulgare) plantations in Turkey. To develop, scald resistant barley varieties, C.R.I.F.C. of Turkey has a large accumulated collection of barley seed sources in hand, but these samples are difficult to be followed and used in the breeding programs due to lack of genetic studies on them. Thus, the objective of this study was to characterize and fingerprint of eighty barley seed sources,...
Evaluation of salt tolerance in sto transformed Arabidopsis thaliana and Nicotiana tabacum plants Selçuk, Feyza; Yücel, Ayşe Meral; Department of Biology (2004) Salinity is one of the limiting factors of crop development. Together with causing water loss from plant tissues, salinity also leads to ion toxicity. Under salt stress, increase in Ca+2 concentration in cytosol can decrease the deleterious effects of stress. The binding of Ca+2 to calmodulin initiates a signaling cascade involving the activation of certain transcription factors like STO and STZ. This signal transduction pathway regulates transport of proteins that control net Na+ influx across the plasma m...
Genetic diversity and structure of Populus nigra populations in two highly fragmented river ecosystems from Turkey Çiftçi, Asiye; Kaya, Zeki (Springer Science and Business Media LLC, 2019-08-01) European black poplar (Populus nigra L.) is an important tree species in terms of social, economic, and ecological interest in Turkey. Although large poplar plantations meet the needs of the economy, natural genetic resources of the species have been highly degraded due to anthropogenic effects such as overexploitation and habitat fragmentations. To assess genetic diversity and structure of fragmented populations, 124 naturally distributed European black poplar trees from two major rivers (Kızılırmak and Gö...
Phylogenetic relationships among Triticum L. and Aegilops L. species as genome progenitors of bread wheat based on sequence diversity in trnT-F region of chloroplast DNA Dizkirici, Ayten; Kansu, Cigdem; Önde, Sertaç; AVCI BİRSİN, MELAHAT; Ozgen, Murat; Kaya, Zeki (Springer Science and Business Media LLC, 2013-12-01) Cultivated wheat, (Triticum aestivum L.), is one of the most important food crops in the world. The Aegilops L. genus is frequently utilized by plant breeders for improving the current wheat cultivars due to their close relationships. Therefore, understanding the phylogenetic relationships among the species of these genera is not only valuable for plant taxonomy, but also for plant breeding efforts. The presented phylogenetic analysis was based on the sequences of trnT-F chloroplast DNA containing three non...

Citation Formats

M. Konus et al., “Molecular adaptations of Helicoverpa armigera midgut tissue under pyrethroid insecticide stress characterized by differential proteome analysis and enzyme activity assays,” COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY D-GENOMICS & PROTEOMICS, pp. 152–162, 2013, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/56912.