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Title: Proteomic analysis of secreted saliva from Russian wheat aphid (Diuraphis noxia Kurd.) biotypes that differ in virulence to wheat

Author
item NICHOLSON, SCOTT
item HARTSON, STEVEN - OKLAHOMA STATE UNIVERSITY
item PUTERKA, GARY

Submitted to: Journal of Proteomics
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 1/27/2012
Publication Date: 3/1/2012
Citation: Nicholson, S.J., Hartson, S.D., Puterka, G.J. 2012. Proteomic analysis of secreted saliva from Russian wheat aphid (Diuraphis noxia Kurd.) biotypes that differ in virulence to wheat. Journal of Proteomics. 75(7):2252-2268.

Interpretive Summary: The Russian wheat aphid (RWA) is an invasive wheat and barley pest causing significant crop losses throughout its range. RWA inflicts damage to its host by the action of toxic salivary components, resulting in symptoms ranging from plant stunting and leaf rolling to death. The salivary compositions of four separate RWA biotypes (strains) were analyzed by three different techniques. One- and two-dimensional electrophoresis demonstrated protein content variance in each examined RWA biotype. Mass spectrometric analysis demonstrated salivary protein variance between biotypes and also identified thirty-four individual proteins among the salivary extracts. This study conclusively determines that RWA salivary proteins differ among biotypes, providing more evidence that salivary content determines phytotoxicity. Many of the proteins observed in RWA saliva are distinct from those observed in other aphids, providing a basis for describing the toxicity of RWA saliva. This work will be useful in understanding RWA toxicity.

Technical Abstract: Thirty-four secreted salivary proteins of Diuraphis noxia, the Russian wheat aphid (RWA), biotypes that differ in virulence to wheat were identified using LC MS/MS. The five major proteins were glucose dehydrogenase, lipophorin, chitinase, CiV16.8g1-like protein, and lava lamp protein. Sixteen proteins varied that varied among biotypes were trehalase, beta-N-acetyl glucosaminidase, glucose dehydrogenase (2), chitinase, lava lamp, retinaldehyde-binding protein, calreticulin, stretchin, aminopeptidase, acetylglucosaminyltransferase, Hydroxymethylglutaryl-CoA lyase, Cytochrome oxidase B, an acyltransferase, Hydroxymethylglutaryl coA lyase, and one protein of unknown function. Fifty-four percent of counted spectra in the proteome were derived from glucose dehydrogenases which could be associated with detoxification or pre-digestion of plant sugars. One-dimensional electrophoresis detected nine protein bands that quantitatively differed ranging from 9 – 70 kDa. Two-dimensional electrophoresis identified six major gel zones where certain proteins quantitatively or qualitatively differed. These analyses confirmed that the salivary proteome differs among RWA biotypes which could lead to a better understanding of the biochemical processes of aphid-plant interactions that lead to phytotoxicity. Our findings confirm that the salivary proteome of the phytotoxic aphid, RWA, differs considerably from those reported for nonphytotoxic aphids such as Acyrthrosiphon pisum Harris.