Tj. Montville et Mec. Bruno, EVIDENCE THAT DISSIPATION OF PROTON MOTIVE FORCE IS A COMMON MECHANISM OF ACTION FOR BACTERIOCINS AND OTHER ANTIMICROBIAL PROTEINS, International journal of food microbiology, 24(1-2), 1994, pp. 53-74
While bacteriocins from lactic acid bacteria (LAB) have generated trem
endous interest among food microbiologists, they are not unique. The b
iosphere is awash with antimicrobial proteins such as colicins, defens
ins, cecropins, and magainins. These proteins share many characteristi
cs. They are low molecular weight, cationic, amphiphilic, tend to aggr
egate and are benign to the producing organism. In cases where the mod
e of action has been investigated, the cell membrane appears to be the
site of action. There is increasing evidence that bacteriocins from m
any bacterial genera also share these characteristics. After a brief i
ntroduction on the significance of LAB bacteriocins, this review provi
des some background on proton motive force. Current studies of mechani
sms for various bacteriocins are reviewed. Evidence is then introduced
that bacteriocins produced by lactic acid bacteria act by the common
mechanism of depleting proton motive force. The role and importance of
energized membranes in this process is examined. These observations a
re linked to literature which demonstrates that many other classes of
antimicrobial proteins act by the same mechanism. Questions regarding
the role of receptor proteins and the physical mechanism by which PMF
is depleted remain unresolved.