Proteomics and Vaccine Design

Recent improvements in high-sensitivity biological mass spectrometry have provided a powerful adjunct to traditional 2D SDS-PAGE gel electrophoresis. The entire complement of proteins expressed by a cell (the proteome) can be defined and becomes a valuable and useful tool for antigen discovery [64]. This kind of approach has already been used to provide insight into the function of a specific subset of the proteome, such as the cell envelope of Salmonella typhimurium [65]. Proteome studies are made even more powerful when applied to an organism whose genome has been sequenced. In a recent study, Montigiani and colleagues used the approach of genomics combined with proteomics to characterize the surface proteins of C. pneumoniae [12]. Other examples where proteomics has also been used to study bacteria pathogenesis and identify vaccine candidates include Streptococcus agalactiae [66, 67] and H. influenzae [68, 69]. Further genome-wide studies are underway for S. aureus and Streptococcus pneumoniae, where integrated proteomic strategies have been successfully applied in the discovery of vaccine antigens. The combination of proteomics and serological analysis allowed the development of SERPA (serological proteome analysis), a technology that has been applied to screen and select new in vivo immunogens, potential vaccine candidates [70].

In conclusion, classical proteomics and immunoproteomics approaches have shown themselves to be a powerful tool for the identification of novel bacterial antigens, for the understanding of protein function and in identifying novel vaccine components. Their use is likely to increase in the years to come.

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