Data set from the proteomic analysis of Bithynia siamensis goniomphalos snails upon infection with the carcinogenic liver fluke Opisthorchis viverrini.

Sattrachai Prasopdee,Alex Loukas,Jason Mulvenna,Cinzia Cantacessi,Javier Sotillo,Thewarach Laha,Rudi Grams,Smarn Tesana

doi:10.1016/j.dib.2014.09.005

Abstract

The snail Bithynia siamensis goniomphalos acts as the first intermediate host for the human liver fluke Opisthorchis viverrini, the major cause of cholangiocarcinoma (CCA) in Northeast Thailand.This data article contains the results obtained from the analysis of the proteins differentially expressed in the snail B. siamensis goniomphalos upon infection with O. viverrini. It contains the data generated from iQuantitator software including a pdf of each sample with a protein׳s relative expression summary and a per-protein detailed analysis of all time points studied and an excel file for each sample containing the raw data from iQuantitator analysis, including ID, mean, standard deviation, credible interval, log2 and description for every protein identified in each of the samples.

Highlights

Data set from the proteomic analysis of Bithynia siamensis goniomphalos snails upon infection with the carcinogenic liver fluke Opisthorchis viverrini
The snail Bithynia siamensis goniomphalos acts as the first intermediate host for the human liver fluke Opisthorchis viverrini, the major cause of cholangiocarcinoma (CCA) in Northeast Thailand
This data article contains the results obtained from the analysis of the proteins differentially expressed in the snail B. siamensis goniomphalos upon infection with O. viverrini

Summary

Sample preparation and protein extraction

Two biological replicates from each studied time point with two headfoot and body samples from two male and two female snails were pooled and placed in a 2 ml microcentrifuge tube with 600 μl of lysis buffer containing 5 M urea, 2 M thiourea, 0.1% SDS, 1% Triton X-100 and 40 mM Tris (pH 7.4). The pellet was discarded and protein supernatant was subsequently precipitated with 10 volumes of cold methanol at À20 C overnight, centrifuged at 8000g for 10 min at 4 C, and air-dried for 5–10 min. Re-dissolved in buffer solution containing 0.5 M triethylammonium bicarbonate (TEAB) and 0.05% SDS, centrifuged at 12,000g for 10 min at 4 1C and protein content was determined by Bradford assay using BSA as a standard. Headfoot and body samples from uninfected snails were used as controls and compared with experimentally infected tissues

Protein digestion and iTRAQ labeling

Peptide OFFGEL fractionation

Findings

Database searching and bioinformatics analysis