Mass spectrometry analysis was performed by the Chemistry & Biochemistry department proteomics core facility using in-house protocols. Briefly, trypsin digested protein samples were acidified with TFA and diluted to 20 ml prior to separation by C18 column (75 um61 mm, LC Packings, Amsterdam, Netherlands) at a flow rate of 30-500 nl/min and introduced into Finnigan LTQ (Thermo electron corporation) through nano spray (2.8 kV). Liquid chromatography mobile phases consisted of Solution A (90% water, 10%methonal, 0.5% formic acid, 0.01% TFA) and Solution B (98% methanol, 2% water, 0.5% formic acid, 0.01% TFA). A 120min linear gradient from 0 to 90% B was typically used. Samples were subjected to nanoelectrospray mass spectrometry using standard procedures and data were analyzed using Sequest (ThermoFinnigan, San Jose, CA; version27, rev. 12) and X! Tandem (www.thegpm.org; version 2007.01.01.1) using the Aedes aegypti database. Scaffold (Proteome Software Inc., Portland, OR) was used to validate MS/ MS based peptide and protein identifications. Sequest identifications required at least DCn scores of greater than 0.08 and XCorr scores of greater than 1.8, 2.5, 3.5 for singly, doubly, triply charged peptides. X! Tandem identifications required at least 2Log(Expect Scores) scores of greater than 3.0.