Meng Zheng

• Assistant Professor at Fordham University
• Postdoctoral Associate at New York University (New York, US)
• Ph.D. in Chemistry from University of Konstanz (Konstanz, Germany)
• M.Sc. in Chemical Biology from Nankai University (Tianjin, China PR)
• B.Sc. in Chemistry from Nankai University (Tianjin, China PR)

Enzymatic transfer reactions of nucleotide/glycosyl molecules are crucial to microbial survival, especially under stressed conditions common in the environment and host cells. Research in my lab utilizes synthetic chemistry, biochemistry, structural biology, biophysical and chemoproteomic approaches to illustrate the enzymatic transfer of nucleotide/glycosyl molecules like ADP-ribose related with antibiotic resistance and bacterial post-translational modification. Further understanding the functional role of such biomolecules and enzymatic transfer reactions can boost the development of novel antimicrobial approach and expand our understanding of bacterial physiology.

Enzymatic transfer of ADP-ribose moiety derived from co-factor NAD⁺ was known as ADP-ribosylation for over 60 years. This process has long been considered an important avenue of protein post-translational modification (PTM) in both eukaryotic and prokaryotic biology. Besides catalyzing modification of both self- and non-self-proteins, bacterial ADP-ribosyltransferases (ARTs) can modify rifamycin antibiotics (RIF), as a resistance mechanism. Rifamycin ARTs (Arr) related resistance has been discovered in various species of bacterial pathogens including Mycobacterium abscesuss, Vibrio cholerea, Klebsiella pneumoniae and E. coli, which creates concern about utilization of RIF as a treatment.