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J Proteomics. 2012 Apr 3;75(7):2252-68. doi: 10.1016/j.jprot.2012.01.031. Epub 2012 Feb 13.

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

Author information

1
USDA-ARS, Plant Science Research Laboratory, Stillwater, OK 74074, United States. scott.nicholson@ars.usda.gov

Abstract

Diuraphis noxia, Russian Wheat Aphid (RWA), biotypes are classified by their differential virulence to wheat varieties containing resistance genes. RWA salivary proteins, unlike those of most aphid species, cause foliar damage and physiological alterations in plants. A comparative proteomic analysis of secreted saliva from four differentially virulent RWA biotypes identified thirty-four individual proteins. The five major proteins were glucose dehydrogenase, lipophorin, chitinase, CiV16.8g1-like, and lava lamp. Fourteen proteins quantitatively varied among biotypes; trehalase, β-N-acetylglucosaminidase (chitinase), two separate glucose dehydrogenases, calreticulin, aminopeptidase, acetylglucosaminyltransferase, hydroxymethylglutaryl-CoA lyase, acyltransferase, ficolin-3, lava lamp, retinaldehyde-binding protein, and two proteins of unknown function. Fifty-four percent of spectral counts were associated with glucose dehydrogenase, which is thought to detoxify plant defensive compounds. One-dimensional electrophoresis detected nine protein bands from 9 to 60 kDa that quantitatively differed. Two-dimensional electrophoresis identified six major gel zones with quantitative and qualitative variance in proteins. Our findings reveal that the salivary proteome of RWA, a phytotoxic aphid, differs considerably from those reported for nonphytotoxic aphids. The potential roles of proteins used in the general plant feeding processes of aphids and those that are potential phytotoxins related to aphid virulence are discussed.

PMID:
22348819
DOI:
10.1016/j.jprot.2012.01.031
[Indexed for MEDLINE]

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