The membrane topology of immunity proteins for the two‐peptide bacteriocins carnobacteriocin XY, lactococcin G, and lactococcin MN shows structural diversity

Abstract

Abstract The two‐peptide bacteriocins produced by Gram‐positive bacteria require two different peptides, present in equimolar amounts, to elicit optimal antimicrobial activity. Producer organisms are protected from their bacteriocin by a dedicated immunity protein. The immunity proteins for two‐peptide bacteriocins contain putative transmembrane domains (TMDs) and might therefore be associated with the membrane. The immunity protein CbnZ for the two‐peptide bacteriocin carnobacteriocin XY (CbnXY) was identified by heterologously expressing the cbnZ gene in sensitive host strains. Using protein topology prediction methods and the dual pho‐lac reporter system, we mapped out the membrane topology of CbnZ, along with those of the immunity proteins LagC and LciM for the two‐peptide bacteriocins lactococcin G and lactococcin MN, respectively. Our results reveal wide structural variety between these immunity proteins that can contain as little as one TMD or as many as four TMDs.

Keywords

• bacteriocin
• immunity protein
• lactic acid bacteria
• membrane protein topology
• two‐peptide