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1.
Insect Mol Biol ; 23(1): 67-77, 2014 Feb.
Article in English | MEDLINE | ID: mdl-24382153

ABSTRACT

Saliva is a critical biochemical interface between aphids and their host plants; however, the biochemical nature and physiological functions of aphid saliva proteins are not fully elucidated. In this study we used a multidisciplinary proteomics approach combining liquid chromatography-electrospray ionization tandem mass spectrometry and two-dimensional differential in-gel electrophoresis/matrix-assisted laser desorption/ionization time-of-flight/mass spectrometry to compare the salivary proteins from three aphid species including Acyrthosiphon pisum, Megoura viciae and Myzus persicae. Comparative analyses revealed variability among aphid salivary proteomes. Among the proteins that varied, 22% were related to DNA-binding, 19% were related to GTP-binding, and 19% had oxidoreductase activity. In addition, we identified a peroxiredoxin enzyme and an ATP-binding protein that may be involved in the modulation of plant defences. Knowledge of salivary components and how they vary among aphid species may reveal how aphids target plant processes and how the aphid and host plant interact.


Subject(s)
Aphids/genetics , Insect Proteins/biosynthesis , Salivary Proteins and Peptides/genetics , Amino Acid Sequence , Animals , Insect Proteins/genetics , Mass Spectrometry , Proteome , Proteomics/methods , Salivary Proteins and Peptides/biosynthesis
2.
Insect Mol Biol ; 17(2): 165-74, 2008 Apr.
Article in English | MEDLINE | ID: mdl-18353105

ABSTRACT

The role of insect saliva in the first contact between an insect and a plant is crucial during feeding. Some elicitors, particularly in insect regurgitants, have been identified as inducing plant defence reactions. Here, we focused on the salivary proteome of the green peach aphid, Myzus persicae. Proteins were either directly in-solution digested or were separated by 2D SDS-PAGE before trypsin digestion. Resulting peptides were then identified by mass spectrometry coupled with database investigations. A homemade database was constituted of expressed sequence tags from the pea aphid Acyrtosiphon pisum and M. persicae. The databases were used to identify proteins related to M. persicae with a nonsequenced genome. This procedure enabled us to discover glucose oxidase, glucose dehydrogenase, NADH dehydrogenase, alpha-glucosidase and alpha-amylase in M. persicae saliva. The presence of these enzymes is discussed in terms of plant-aphid interactions.


Subject(s)
Aphids/metabolism , Insect Proteins/metabolism , Proteomics/methods , Salivary Proteins and Peptides/metabolism , Amylases/metabolism , Animals , Aphids/enzymology , Electrophoresis, Polyacrylamide Gel , Glucose 1-Dehydrogenase/metabolism , Glucose Oxidase/metabolism , Insect Proteins/chemistry , NADH Dehydrogenase/metabolism , Salivary Proteins and Peptides/chemistry , Spectrometry, Mass, Electrospray Ionization , Tandem Mass Spectrometry , Trypsin/metabolism , alpha-Glucosidases/metabolism
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