Collaborating with Prof. DENG Jiaoyu from Wuhan Institute of Virology of Chinese Academy of Sciences, researchers performed a global acetylome analysis on M. tuberculosis H37Ra through the combined use of protein/peptide prefractionation, antibody enrichment, and LC-MS/MS analysis. A total of 226 acetylation sites in 137 proteins were found to be involved in various biological processes, such as glycolysis/gluconeogenesis, citrate cycle and fatty acid metabolism. Further functional studies showed that lysine acetylation may play an important role in colony morphology, biofilm formation and tolerance to heat stress in M. tuberculosis H37Ra. It is the first time that lysine acetylation was found to block the immunogenicity.
The findings not only serve as important resource for the functional analysis of lysine acetylation in M. tuberculosis, but also facilitate the elucidation of the entire metabolic networks in this life-threatening pathogen. Relevant results were published in the Journal of Proteome Research and in Molecular & cellular proteomics.
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