Advanced techniques and high-throughput protein analysis have led proteomics to substantive progress in the understanding of bacterial-host interactions. Mass spectrometry (MS)-based proteomics have been a central methodology in the discovery of new protein involved in the infectious process that leads to thousands of deaths every year. The discovery of novel protein targets, together with de novo drug design, improves the accuracy of early diagnosis, leading to improved new treatments. MS-based proteomics has also been widely applied to structural biology, where proteomic investigation is being used to improve knowledge on the relationship between protein sequence, structure, and function. Thus, the search for therapeutic targets for infectious diseases using these cutting-edge technologies represents the new frontiers for proteomics applications in biomedicine and pharmacology. In this review, the main classical gel-based methods (2-DE, DIGE) are discussed, as well as the advances of gel-free quantitative proteomic techniques, from metabolic and chemical labeling (SILAC, iTRAQ, ICAT, (16)O/(18)O, QconCAT) to nonlabeling (MS spectra counting and peak integration) strategies. Together, these proteomic methods are currently being used in the quest for tailor-made pharmaceutical and biomedical research for bacterial control, where advances in these analytical methods may represent greater improvements in the treatment of a number of infectious diseases.
Keywords: Bacteria; Drug design; Infectious diseases; Mass spectrometry; Proteome.
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