Abstract
Recent developments in pharmaceutical technology allow systematic investigation of molecules operating in a living cell, facilitating identification of key players, which show potential as novel drug targets. One of the tools that has emerged for identifying potential antigens for use as vaccines against infectious diseases is time-course proteome analysis. The model virulent microorganism Candida albicans has been well studied in terms of both physiological characteristics and clinical aspects for developing pharmaceutics in treatments. In this article, we review a time-course proteome study of C. albicans during adaptation to a serum. Furthermore, we introduce a novel biotechnological strategy for developing vaccines using characteristic proteins that have been identified as virulence-related molecules.
Highlights
Infectious disease is a major cause of morbidity and mortality
Extracted proteins were labeled using tandem mass tagging (TMT) and evaluated, and LC-MS/MS analysis was performed with a long monolithic silica capillary column (470 cm), using the proteome samples taken at 0 min on YPD as a control
We suggest that C. albicans employed the following adaptation strategy: first, C. albicans tuned its proteome to adapt to a new environment, in which most proteins were upregulated 2-fold higher than has been suggested by previous studies [23]
Summary
Infectious disease is a major cause of morbidity and mortality. Following the development of penicillin [1], the first antibiotic, public health has been greatly improved through the development of subsequent antibiotics. Extracted proteins were labeled using tandem mass tagging (TMT) and evaluated, and LC-MS/MS analysis was performed with a long monolithic silica capillary column (470 cm), using the proteome samples taken at 0 min on YPD as a control. Other proteins in the FBS series showed moderate abundance changes [19] Based on these results, we suggest that C. albicans employed the following adaptation strategy: first, C. albicans tuned its proteome to adapt to a new environment, in which most proteins were upregulated 2-fold higher than has been suggested by previous studies [23]. C. albicans malate dehydrogenase (Mdh1p) was identified by the time-course proteome studies discussed above as the group 4 (Figure 3), and was thought to be a candidate for a vaccine against candidiasis because it was identified through every periods without large variation in relative abundance. An investigation of time-course variation in C. albicans under serum-containing conditions to identify virulencerelated molecules could provide novel and effective antigenic proteins
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