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Tissue and Life Stage Specificity of Glutathione S-Transferase Expression in the Hessian Fly, Mayetiola destructor: Implications for Resistance to Host Allelochemicals

Two new Delta and Sigma glutathione S-transferases (GSTs) in the Hessian fly, Mayetiola destructor (Diptera: Cecidomyiidae), were characterized and transcription profiles described. The deduced amino acid sequences for the two M. destructor Delta GSTs (MdesGST-1 and MdesGST-3) showed high similarity...

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Autores principales: Mittapalli, Omprakash, Neal, Jonathan J., Shukle, Richard H.
Formato: Texto
Lenguaje:English
Publicado: University of Wisconsin Library 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2999413/
https://www.ncbi.nlm.nih.gov/pubmed/20307234
http://dx.doi.org/10.1673/031.007.2001
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author Mittapalli, Omprakash
Neal, Jonathan J.
Shukle, Richard H.
author_facet Mittapalli, Omprakash
Neal, Jonathan J.
Shukle, Richard H.
author_sort Mittapalli, Omprakash
collection PubMed
description Two new Delta and Sigma glutathione S-transferases (GSTs) in the Hessian fly, Mayetiola destructor (Diptera: Cecidomyiidae), were characterized and transcription profiles described. The deduced amino acid sequences for the two M. destructor Delta GSTs (MdesGST-1 and MdesGST-3) showed high similarity with other insect Delta GSTs including the conserved catalytic serine residue. The deduced amino acid sequence for the M. destructor Sigma GST (MdesGST-2) showed high similarity with other insect Sigma GSTs including the conserved glutathione and substrate binding sites. Quantitative tissue expression analysis showed that mRNA levels for MdesGST-1 were predominant in fat body, whereas for MdesGST-2 and MdesGST-3 expression was predominant in the midgut. Temporal expression during development showed peak mRNA levels for MdesGST-1 during larval development, but in the pupal stage for MdesGST-2. MdesGST-3 showed a constitutive expression pattern throughout development. M. destructor feeds on wheat, and expression analysis after feeding indicated that mRNA levels for MdesGST-1 were significantly higher in incompatible interactions in which larvae fed on resistant wheat, while MdesGST-3 was significantly higher in compatible interactions when larvae fed on susceptible wheat. MdesGST-2 showed an equivalent expression pattern during both interactions. These results suggest that the M. destructor Delta GSTs are important in detoxifying wheat allelochemicals during feeding, while Sigma GST participates in metabolism of endogenous substrates.
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spelling pubmed-29994132010-12-09 Tissue and Life Stage Specificity of Glutathione S-Transferase Expression in the Hessian Fly, Mayetiola destructor: Implications for Resistance to Host Allelochemicals Mittapalli, Omprakash Neal, Jonathan J. Shukle, Richard H. J Insect Sci Article Two new Delta and Sigma glutathione S-transferases (GSTs) in the Hessian fly, Mayetiola destructor (Diptera: Cecidomyiidae), were characterized and transcription profiles described. The deduced amino acid sequences for the two M. destructor Delta GSTs (MdesGST-1 and MdesGST-3) showed high similarity with other insect Delta GSTs including the conserved catalytic serine residue. The deduced amino acid sequence for the M. destructor Sigma GST (MdesGST-2) showed high similarity with other insect Sigma GSTs including the conserved glutathione and substrate binding sites. Quantitative tissue expression analysis showed that mRNA levels for MdesGST-1 were predominant in fat body, whereas for MdesGST-2 and MdesGST-3 expression was predominant in the midgut. Temporal expression during development showed peak mRNA levels for MdesGST-1 during larval development, but in the pupal stage for MdesGST-2. MdesGST-3 showed a constitutive expression pattern throughout development. M. destructor feeds on wheat, and expression analysis after feeding indicated that mRNA levels for MdesGST-1 were significantly higher in incompatible interactions in which larvae fed on resistant wheat, while MdesGST-3 was significantly higher in compatible interactions when larvae fed on susceptible wheat. MdesGST-2 showed an equivalent expression pattern during both interactions. These results suggest that the M. destructor Delta GSTs are important in detoxifying wheat allelochemicals during feeding, while Sigma GST participates in metabolism of endogenous substrates. University of Wisconsin Library 2007-04-09 /pmc/articles/PMC2999413/ /pubmed/20307234 http://dx.doi.org/10.1673/031.007.2001 Text en © 2007 http://creativecommons.org/licenses/by/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Article
Mittapalli, Omprakash
Neal, Jonathan J.
Shukle, Richard H.
Tissue and Life Stage Specificity of Glutathione S-Transferase Expression in the Hessian Fly, Mayetiola destructor: Implications for Resistance to Host Allelochemicals
title Tissue and Life Stage Specificity of Glutathione S-Transferase Expression in the Hessian Fly, Mayetiola destructor: Implications for Resistance to Host Allelochemicals
title_full Tissue and Life Stage Specificity of Glutathione S-Transferase Expression in the Hessian Fly, Mayetiola destructor: Implications for Resistance to Host Allelochemicals
title_fullStr Tissue and Life Stage Specificity of Glutathione S-Transferase Expression in the Hessian Fly, Mayetiola destructor: Implications for Resistance to Host Allelochemicals
title_full_unstemmed Tissue and Life Stage Specificity of Glutathione S-Transferase Expression in the Hessian Fly, Mayetiola destructor: Implications for Resistance to Host Allelochemicals
title_short Tissue and Life Stage Specificity of Glutathione S-Transferase Expression in the Hessian Fly, Mayetiola destructor: Implications for Resistance to Host Allelochemicals
title_sort tissue and life stage specificity of glutathione s-transferase expression in the hessian fly, mayetiola destructor: implications for resistance to host allelochemicals
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2999413/
https://www.ncbi.nlm.nih.gov/pubmed/20307234
http://dx.doi.org/10.1673/031.007.2001
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