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Physiological and Molecular Alterations Promoted by Schizotetranychus oryzae Mite Infestation in Rice Leaves.

Authors :
Buffon G
Blasi ÉA
Adamski JM
Ferla NJ
Berger M
Santi L
Lavallée-Adam M
Yates JR 3rd
Beys-da-Silva WO
Sperotto RA
Source :
Journal of proteome research [J Proteome Res] 2016 Feb 05; Vol. 15 (2), pp. 431-46. Date of Electronic Publication: 2015 Dec 30.
Publication Year :
2016

Abstract

Infestation of phytophagous mite Schizotetranychus oryzae in rice causes critical yield losses. To better understand this interaction, we employed Multidimensional Protein Identification Technology (MudPIT) approach to identify differentially expressed proteins. We detected 18 and 872 unique proteins in control and infested leaves, respectively, along with 32 proteins more abundant in control leaves. S. oryzae infestation caused decreased abundance of proteins related to photosynthesis (mostly photosystem II-related), carbon assimilation and energy production, chloroplast detoxification, defense, and fatty acid and gibberellin synthesis. On the contrary, infestation caused increased abundance of proteins involved in protein modification and degradation, gene expression at the translation level, protein partitioning to different organelles, lipid metabolism, actin cytoskeleton remodeling, and synthesis of jasmonate, amino acid, and molecular chaperones. Our results also suggest that S. oryzae infestation promotes cell-wall remodeling and interferes with ethylene biosynthesis in rice leaves. Proteomic data were positively correlated with enzymatic assays and RT-qPCR analysis. Our findings describe the protein expression patterns of infested rice leaves and suggest that the acceptor side of PSII is probably the major damaged target in the photosynthetic apparatus. These data will be useful in future biotechnological approaches aiming to induce phytophagous mite resistance in rice.

Details

Language :
English
ISSN :
1535-3907
Volume :
15
Issue :
2
Database :
MEDLINE
Journal :
Journal of proteome research
Publication Type :
Academic Journal
Accession number :
26667653
Full Text :
https://doi.org/10.1021/acs.jproteome.5b00729