African Journal of
Agricultural Research

  • Abbreviation: Afr. J. Agric. Res.
  • Language: English
  • ISSN: 1991-637X
  • DOI: 10.5897/AJAR
  • Start Year: 2006
  • Published Articles: 6693

Full Length Research Paper

Comparative proteomic analyses of Anticarsia gemmatalis and Spodoptera frugiperda guts

Fariba Mehrkhou1, Ali Asghar Talebi2, Mahmoud Ghasemi Kochameshgi3, Vahid Hosseininaveh3, Elizabete de Souza Cândido4, Bernardo Petriz4, Simoni Campos Dias4, Maria Elita Batista Castro5, Angela Mehta5 and Octavio Luiz Franco4*
1Department of Plant Protection, Faculty of Agriculture, Urmia University, P. O. Box: 57153-165, West Azarbayjan, Iran. 2Department of Entomology, Faculty of Agriculture, Tarbiat Modares University, P. O. Box: 14115-336, Tehran, Iran. 3Department of Plant Protection, College of Agricultural Sciences and Natural Resources, University of Tehran, Karaj, Iran. 4Center for Proteomic and Biochemical Analyses, Post-Graduate Program in Genomic Sciences and Biotechnology, Universidade Católica de Brasília, Campus Avançado Asa Norte - SGAN 916 Avenida W5 - CEP: 70790-160 - Brasilia – DF, Brazil. 5Embrapa Genetic Resources and Biotechnology, P. O. Box: 02372, CEP: 70770-917- Brasilia-DF, Brazil.
Email: [email protected]

  •  Accepted: 17 May 2012
  •  Published: 12 June 2012

Abstract

Anticarsia gemmatalis and Spodoptera frugiperda (Lepidoptera: Noctuidae) are serious defoliators of a number of crops. In order to better understand the digestion process of these pests and considering that the midgut is one of the most important and attractive targets for biological pesticides, this report shows the evaluation of midgut proteins from A. gemmatalis and S. frugiperda by proteomic analyses. Larval midguts were removed and total proteins (approximately 650 µg) were extracted and further submitted to two-dimensional electrophoresis (2-DE). Proteins were identified by tandem mass spectrometry (MS/MS) including catalase, enolase, glyceraldehyde-3-phosphate dehydrogenase, arginine kinase, pyrophosphatase and farnesoic acid O-methyl transferase. All proteins identified seem to be involved in insect development in different ways, being directly involved in their growth or used in metabolic pathways that may influence pest development. The identification of those proteins could contribute to a better understanding of pest physiology, leading to the development of novel strategies for pest management. In short, the identification of proteins by 2D may lead to the use of new approaches for pest management.

 

Key words: Anticarsia gemmatalisSpodoptera frugiperda, proteomics, mass spectrometry (MS).