Premium
Maturation pathway of nisin and other lantibiotics: post‐translationally modified antimicrobial peptides exported by Gram‐positive bacteria
Author(s) -
Vos Willem M.,
Kuipers Oscar P.,
Meer Jan Roelof,
Siezen Roland J.
Publication year - 1995
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1995.mmi_17030427.x
Subject(s) - lantibiotics , nisin , lactococcus lactis , antimicrobial peptides , biology , bacteriocin , biochemistry , bacteria , signal peptide , antimicrobial , peptide , peptide sequence , microbiology and biotechnology , gene , lactic acid , genetics
Lantibiotics form a family of highly modified peptides which are secreted by several Gram‐positive bacteria. They exhibit antimicrobial activity, mainly against other Gram‐positive bacteria, by forming pores in the cellular membrane. These antimicrobial peptides are ribosomally synthesized and contain leader peptides which do not show the characteristics of signal sequences. Several amino acid residues of the precursor lantibiotic are enzymatically modified, whereafter secretion and processing of the leader peptide takes place, yielding the active antimicrobial substance. For several lantibiotics the gene clusters encoding biosynthetic enzymes, translocator proteins, self‐protection proteins, processing enzymes and regulatory proteins have been identified. This MicroReview describes the current knowledge about the biosynthetic, immunity and regulatory processes leading to lantibiotic production. Most of the attention is focused on the lantibiotic nisin, which is produced by the food‐grade bacterium Lactococcus lactis and is widely used as a preservative in the food industry.