Submitted to: Entomological Society of America Annual Meeting
Publication Type: Abstract only
Publication Acceptance Date: 8/24/2007
Publication Date: 12/10/2007
Publication URL: http://esa.confex.com/esa/2007/techprogram/paper_30926.htm
Citation: Hasan, A., Backus, E.A., Schreiber, F. 2007. Salivary Secretions of the Glassy-winged Sharpshooter, Homalodisca vitripennis: Novel Method of Collection and Protein Profile [abstract]. Entomological Society of America Annual Meeting. Available: http://esa.confex.com/esa/2007/techprogram/paper_30926.htm Interpretive Summary:
Technical Abstract: The glassy-winged sharpshooter, Homalodisca vitripennis Takiya (Hemiptera: Cicadellidae) is a xylophagous leafhopper that efficiently transmits Xylella fastidiosa, causative agent of a variety of scorch diseases such as Pierce’s Disease of grapes. The transmission mechanism of X. fastidiosa by the sharpshooter is presently unknown, but recent research suggests that salivation during feeding may be involved. The objective of this study was to begin biochemical investigation of salivary secretions, by first developing a novel method of collection and subsequently analyzing the profile of collected salivary proteins. The new collection method involved brushing the sharpshooter’s labrum and clypeus using a camel hair brush and collecting the secreted salivary bubble using glass fiber paper. The collected salivary secretion samples compared with the total extract of dissected salivary glands were analyzed using SDS-PAGE. The saliva collection method proved to be more efficient than traditional techniques using an artificial diet as a medium to collect saliva. Also, this method allowed observation in real time of the separation of the salivary sheath and watery saliva, by gradual solidification of part of the salivary secretion. In addition, small portions of solid sheath solubilized when more salivary secretions were produced. SDS-PAGE revealed that salivary secretions contain a large mixture of proteins. The most abundant salivary protein was found to have a molecular weight of 12kD. Research is underway to characterize major protein components of H. vitripennis salivary secretions.