Abstract
The brown planthopper (BPH), Nilaparvata lugens (Stål), is a destructive pest that poses a significant threat to rice plants worldwide. To explore how BPHs adapt to the resistant rice variety, we analyzed proteomics profiles of two virulent N. lugens populations. We focused on Biotype Y, which can survive on the moderately resistant rice variety YHY15, and Biotype I, which can survive on the susceptible rice variety TN1. We performed protein quantitation using the isobaric tag for relative and absolute quantification (iTRAQ) and then compared the expression patterns between two virulent N. lugens populations and found 258 differentially expressed proteins (DEPs). We found that 151 of the DEPs were up-regulated, while 107 were down-regulated. We evaluated transcript levels of 8 expressed genes from the iTRAQ results by qRT-PCR, which revealed transcriptional changes that were consistent with the changes at the protein level. The determination of the protein changes in two virulent N. lugens populations would help to better understanding BPH adaptation to resistant rice varieties and facilitate the better design of new control strategies for host defense against BPH.
Highlights
Proteomics is the study of proteins and their impact on cells, tissues and organisms
Proteomic studies based on two-dimensional electrophoresis were used to identify differentially expressed proteins (DEPs), including those related to rapid cold stress response in Lissorhoptrus oryzophilus [1] and immune response in Triatoma dimidiate [2]
Proteins that were differentially expressed between brown planthopper (BPH)-YHY15 and BPH-TN1 were evaluated by isobaric tag for relative and absolute quantification (iTRAQ) labeling and quantified by liquid chromatography-mass spectrometry analysis (Fig 1)
Summary
Proteomics is the study of proteins and their impact on cells, tissues and organisms. Proteomic studies based on two-dimensional electrophoresis were used to identify differentially expressed proteins (DEPs), including those related to rapid cold stress response in Lissorhoptrus oryzophilus [1] and immune response in Triatoma dimidiate [2]. These new approaches include the isobaric tag for relative and absolute quantification (iTRAQ), which is more reliable than two-dimensional electrophoresis [3].
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