Class IIa bacteriocins: biosynthesis, structure and activity

FEMS Microbiol Rev. 2000 Jan;24(1):85-106. doi: 10.1111/j.1574-6976.2000.tb00534.x.

Abstract

In the last decade, a variety of ribosomally synthesized antimicrobial peptides or bacteriocins produced by lactic acid bacteria have been identified and characterized. As a result of these studies, insight has been gained into fundamental aspects of biology and biochemistry such as producer self protection, membrane-protein interactions, and protein modification and secretion. Moreover, it has become evident that these peptides may be developed into useful antimicrobial additives. Class IIa bacteriocins can be considered as the major subgroup of bacteriocins from lactic acid bacteria, not only because of their large number, but also because of their activities and potential applications. They have first attracted particular attention as listericidal compounds and are now believed to be the next in line if more bacteriocins are to be approved in the future. The present review attempts to provide an insight into general knowledge available for class IIa bacteriocins and discusses common features and recent findings concerning these substances.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Bacteria / drug effects
  • Bacterial Proteins / immunology
  • Bacteriocins / chemistry*
  • Bacteriocins / genetics
  • Bacteriocins / metabolism*
  • Bacteriocins / pharmacology
  • Consensus Sequence
  • Genes, Bacterial / genetics
  • Gram-Positive Bacteria / drug effects
  • Gram-Positive Bacteria / genetics
  • Gram-Positive Bacteria / metabolism
  • Lactic Acid / metabolism
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Open Reading Frames
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Structure-Activity Relationship

Substances

  • Bacterial Proteins
  • Bacteriocins
  • Lactic Acid