The bacterial genus Corynebacteria contains several pathogenic species that 
cause diseases such as diphtheria in humans and "cheesy gland" in goats and 
sheep. Thus, identifying new therapeutic targets to treat Corynebacteria 
infections is both medically and economically important. CG2496, a functionally 
uncharacterized protein from Corynebacterium glutamicum, was evaluated using an 
NMR ligand-affinity screen. A total of 11 compounds from a library of 460 
biologically active compounds were shown to selectively bind CG2496 in a highly 
conserved region of the protein. The best binder was identified to be 
methiothepin (KD =54 ± 19 µM), an FDA-approved serotonin receptor antagonist. 
Methiothepin was also shown to inhibit the growth of C. glutamicum, but not 
bacteria that lack CG2496 homologs. Our results suggest that CG2496 is a novel 
therapeutic target and methiothepin is a potential lead compound or structural 
scaffold for developing new antibiotics specifically targeting Corynebacteria.