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Konus, M.* ; Koy, C.* ; Mikkat, S.* ; Kreutzer, M.* ; Zimmermann, R. ; Iscan, M.* ; Glocker, M.O.*

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

Comp. Biochem. Physiol. D-Genomics Proteomics 8, 152-162 (2013)
DOI PMC
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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. (C) 2013 Elsevier Inc. All rights reserved.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Detoxification ; Energy Metabolism ; Comparative Proteomics ; Mass Spectrometry ; Glutathione S-transferases; Glutathione S-transferases ; In-vitro Metabolism ; Caenorhabditis-elegans ; Nilaparvata-lugens ; Expressed Proteins ; Hubner Lepidoptera ; Dependent Changes ; Cotton Bollworm ; West-africa ; Resistance
Sprache englisch
Veröffentlichungsjahr 2013
HGF-Berichtsjahr 2013
ISSN (print) / ISBN 1744-117X
e-ISSN 1878-0407
Zeitschrift Comparative Biochemistry and Physiology. Part D: Genomics and Proteomics
Quellenangaben Band: 8, Heft: 2, Seiten: 152-162 Artikelnummer: , Supplement: ,
Verlag Elsevier
Begutachtungsstatus Peer reviewed
Institut(e) Cooperation Group Comprehensive Molecular Analytics (CMA)
POF Topic(s) 30202 - Environmental Health
Forschungsfeld(er) Environmental Sciences
PSP-Element(e) G-504500-001
PubMed ID 23685472
DOI 10.1016/j.cbd.2013.04.001
WOS ID WOS:000320206000006
Scopus ID 84878086211
Erfassungsdatum 2013-07-12
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