REVIEW: Pediocin-Like Antimicrobial Peptides of Bacteria

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S. V. Balandin¹, E. V. Sheremeteva¹, and T. V. Ovchinnikova^1,a*

¹Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia

^* To whom correspondence should be addressed.

Received August 6, 2018; Revised October 11, 2018; Accepted October 11, 2018

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Bacteriocins are bacterial antimicrobial peptides that, unlike classical peptide antibiotics, are products of ribosomal synthesis and usually have a narrow spectrum of antibacterial activity against species closely related to the producers. Pediocin-like bacteriocins (PLBs) belong to the class IIa of the bacteriocins of Gram-positive bacteria. PLBs possess high activity against pathogenic bacteria from Listeria and Enterococcus genera. Molecular target for PLBs is a membrane protein complex – bacterial mannose-phosphotransferase. PLBs can be synthesized by components of symbiotic microflora and participate in the maintenance of homeostasis in various compartments of the digestive tract and on the surface of epithelial tissues contacting the external environment. PLBs could give a rise to a new group of antibiotics of narrow spectrum of activity.

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KEY WORDS: antimicrobial peptides, bacteriocins, pediocin-like antimicrobial peptides, antibiotic resistance, mannose phosphotransferase

DOI: 10.1134/S000629791905002X

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