Protein O-mycoloylation is a unique post-translational lipidation that was recently discovered in Corynebacterium. Beyond the two porin proteins originally determined to be O-mycoloylated, PorA and PorH, the scope of this modification in Corynebacterium and related bacteria is unknown. Here, we demonstrate that an alkyne-modified trehalose monomycolate chemical reporter allows metabolic labeling of O-mycoloylated proteins in whole cells of C. glutamicum. In combination with click chemistry, this chemical reporter enabled the detection and identification of the known O-mycoloylated proteins PorA and PorH, as well as several other candidate O-mycoloylated proteins, including the outer-membrane porin protein PorB. This strategy will facilitate future efforts to identify and characterize O-mycoloylated proteins in Corynebacterium and related genera

Utilization of mycobacteria carbohydrate metabolic pathways to develop chemical reporters for detecting and identifying O-mycoloylated proteins in mycobacteria

254th National Meeting (2017)

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