Lantibiotics are post translationally modified peptides and certain modifications occur during biosynthesis including the dehydration of some amino acids to form Lanthionine ring. When the structural gene encoding lantibiotic production was cloned alone and then expressed it gave no inhibitory activity (Not modified). Is there a way to clone the gene encoding the modification enzyme to express it ? Maybe after that we can incubate the modification enzyme with the unmodified peptide to give biologically active lantibiotic.
From my brief involvement in studying the biosynthesis of thiostrepton (like lantibiotics, also highly modified), it's really difficult to produce it heterologously. First we need to include the post-translational modifying enzymes (either clone the whole gene cluster, unlikely to succeed, or if possible combining the genes in several duet vectors). Then, we need to insert also the precursor (we have to think about maturation of the peptide in the end). A problem may arise when the mature peptide is becoming toxic to the host. In my case at that time, the precursor was unstable and quickly degraded.
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