Mapping Anopheles stephensi midgut proteome using high-resolution mass spectrometry

• Published in: Data in brief 2018-04, Vol.17, p.1295-1303
• Main Authors: Mohanty, Ajeet Kumar, Dey, Gourav, Kumar, Manish, Sreenivasamurthy, Sreelakshmi K., Garg, Sandeep, Prasad, T. S. Keshava, Kumar, Ashwani
• Format: Article
• Language: English
• Subjects: Proteomics and Biochemistry
• ISSN: 2352-3409; 2352-3409
• DOI: 10.1016/j.dib.2018.02.028

Anopheles stephensi Liston is one of the major vectors of malaria in urban areas of India. Midgut plays a central role in the vector life cycle and transmission of malaria. Because gene expression of An. stephensi midgut has not been investigated at protein level, an unbiased mass spectrometry-based proteomic analysis of midgut tissue was carried out. Midgut tissue proteins from female An. stephensi mosquitoes were extracted using 0.5% SDS and digested with trypsin using two complementary approaches, in-gel and in-solution digestion. Fractions were analysed on high-resolution mass spectrometer, which resulted in acquisition of 494,960 MS/MS spectra. The MS/MS spectra were searched against protein database comprising of known and predicted proteins reported in An. stephensi using Sequest and Mascot software. In all, 47,438 peptides were identified corresponding to 5,709 An. stephensi proteins. The identified proteins were functionally categorized based on their cellular localization, biological processes and molecular functions using Gene Ontology (GO) annotation. Several proteins identified in this data are known to mediate the interaction of the Plasmodium with vector midgut and also regulate parasite maturation inside the vector host. This study provides information about the protein composition in midgut tissue of female An. stephensi, which would be useful in understanding vector parasite interaction at molecular level and besides being useful in devising malaria transmission blocking strategies. The data of this study is related to the research article “Integrating transcriptomics and proteomics data for accurate assembly and annotation of genomes”.