Lantibiotics, a family of bacterial antibiotics, are very active in the singlenanomolar range, thus significantly more powerful than their more conventional counterparts, an attribute that reduces the chance of unwanted side effects and which indicates that the molecular target must play an essential role in bacterial viability. They are unusual in requiring posttranslational modification by dedicated modification enzymes. In a search of published genome sequences, Colin Hill of University College Cork, Cork, Ireland, and Paul D. Cotter, recently recruited to Teagasc Moorepark Food Research Centre, Fermoy, Ireland, and their collaborators identified more than 60 potential modification enzymes. (Teagasc is the Gaelic word for "instruction.") They then searched for nearby genes which could encode novel lantibiotics, and for other proteins involved in lantibiotic export and immunity, ultimately identifying several "likely candidates which appear to have the necessary machinery required to synthesize and export a lantibiotic," says Hill. "We were able to confirm production of a lantibiotic which is active against several pathogens, including the MRSA superbug," says Hill. "We were even able to predict the structure of this novel lantibiotic, which we named lichenicidin. Given the increasing number of publicly available genome sequences, we recommend this in silico approach as a useful alternative to traditional screening."