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lantibiotics applications, lantibiotics
Lantibiotics are a class of peptide antibiotics that contain the characteristic polycyclic thioether amino acids lanthionine or methyllanthionine, as well as the unsaturated amino acids dehydroalanine and 2-aminoisobutyric acid

Lanthionine is composed of two alanine residues that are crosslinked on their β-carbon atoms by a thioether monosulfide linkage

Lantibiotics are produced by a large number of Gram-positive bacteria such as Streptococcus and Streptomyces to attack other Gram-positive bacteria, and as such, they are considered a member of the bacteriocins Bacteriocins are classified according to their extent of posttranslational modification The lantibiotics are a class of more extensively modified bacteriocins, also called Class I bacteriocins Bacteriocins for which disulfide bonds are the only modification to the peptide are Class II bacteriocins

Lantibiotics are well studied because of the commercial use of these bacteria in the food industry for making dairy products such as cheese

Nisin and epidermin are members of a family of lantibiotics that bind to lipid II, a cell wall precursor lipid component of target bacteria and disrupt cell wall production The duramycin family of lantibiotics binds phosphoethanolamine in the membranes of its target cells and seem to disrupt several physiological functions


  • 1 History
  • 2 Classification
    • 21 Examples
  • 3 Biosynthesis
  • 4 Mechanism of action
  • 5 Application
    • 51 Food preservation
    • 52 Veterinary antibiotic
    • 53 Clinical antibiotic
  • 6 Databases
  • 7 References
  • 8 Further reading
  • 9 External links


The name lantibiotics was introduced in 1988 as an abbreviation for "lanthionine-containing peptide antibiotics" The first structures of these antimicrobial agents were produced by pioneering work by Gross and Morell in the late 1960s and early 1970s, thus marking the formal introduction of lantibiotics Since then, lantibiotics such as nisin have been used auspiciously for food preservation and have yet to encounter significant bacterial resistance These attributes of lantibiotics have led to more detailed research into their structures and biosynthetic pathways


  • Type A lantibiotics are long flexible molecules - eg, nisin, bisin, subtilin, epidermin, gallidermin Subgroup AI includes mutacin II; subgroup AII includes mutacin I and III
  • Type B lantibiotics are globular - eg, mersacidin actagardine, duramycin, and cinnamycin

Some contain 2 peptides, eg haloduracin


Lantibiotic Type # of
# of
thioether links
A 34 5 0
A 21 3 1
mersacidin B 20 4
actagardine B 19 4 0
B 19 3 1
Sublancin 168   37 1 2
Plantaricin C B 27 4 0

Sublancin may be an S-linked glycopeptide


They are synthesised with a leader polypeptide sequence that is removed only during the transport of the molecule out of the synthesising cell They are synthesized by ribosomes, which distinguishes them from most natural antibiotics There are four known enzymes lanthipeptide synthetases responsible for producing lanthionine rings

Mechanism of action

Lantibiotics show substantial specificity for some components eg, lipid II of bacterial cell membranes especially of Gram-positive bacteria Type A lantibiotics kill rapidly by pore formation, type B lantibiotics inhibit peptidoglycan biosynthesis They are active in very low concentrations


Food preservation

Lantibiotics are produced by Gram-positive bacteria and show strong antimicrobial action toward a wide range of other Gram-positive bacteria As such, they have become attractive candidates for use in food preservation by inhibiting pathogens that cause food spoilage and the pharmaceutical industry to prevent or fight infections in humans or animals

Veterinary antibiotic

Duramycin is used for chickens

Clinical antibiotic

One type known as B lantibiotic NVB302 entered phase 1 clinical trials in 2011 for use against Clostridium difficile, and reported good results in 2012


BACTIBASE is an open-access database for bacteriocins including lantibiotics LANTIBASE is a lantibiotic specific resource


  1. ^ Chatterjee C, Paul M, Xie L, van der Donk WA February 2005 "Biosynthesis and mode of action of lantibiotics" Chem Rev 105 2: 633–84 doi:101021/cr030105v PMID 15700960 
  2. ^ a b Kellner R, Jung G, Hörner T, Zähner H, Schnell N, Entian KD, Götz F October 1988 "Gallidermin: a new lanthionine-containing polypeptide antibiotic" Eur J Biochem 177 1: 53–9 doi:101111/j1432-10331988tb14344x PMID 3181159 
  3. ^ a b Sass P, Jansen A, Szekat C, Sass V, Sahl HG, Bierbaum G 2008 "The lantibiotic mersacidin is a strong inducer of the cell wall stress response of Staphylococcus aureus" BMC Microbiol 8: 186 doi:101186/1471-2180-8-186 PMC 2592248  PMID 18947397 
  4. ^ Brötz H, Bierbaum G, Markus A, Molitor E, Sahl HG March 1995 "Mode of action of the lantibiotic mersacidin: inhibition of peptidoglycan biosynthesis via a novel mechanism" Antimicrob Agents Chemother 39 3: 714–9 doi:101128/AAC393714 PMC 162610  PMID 7793878 
  5. ^ a b Makino A, Baba T, Fujimoto K, Iwamoto K, Yano Y, Terada N, Ohno S, Sato SB, Ohta A, Umeda M, Matsuzaki K, Kobayashi T January 2003 "Cinnamycin Ro 09-0198 promotes cell binding and toxicity by inducing transbilayer lipid movement" J Biol Chem 278 5: 3204–9 doi:101074/jbcM210347200 PMID 12446685 
  6. ^ Cooper LE, McClerren AL, Chary A, van der Donk WA October 2008 "Structure-activity relationship studies of the two-component lantibiotic haloduracin" Chem Biol 15 10: 1035–45 doi:101016/jchembiol200807020 PMC 2633096  PMID 18940665 
  7. ^ Stein T May 2005 "Bacillus subtilis antibiotics: structures, syntheses and specific functions" Mol Microbiol 56 4: 845–57 doi:101111/j1365-2958200504587x PMID 15853875 
  8. ^ Oman TJ, Boettcher JM, Wang H, Okalibe XN, van der Donk WA February 2011 "Sublancin is not a lantibiotic but an S-linked glycopeptide" Nat Chem Biol 7 2: 78–80 doi:101038/nchembio509 PMC 3060661  PMID 21196935 
  9. ^ Siegers K, Heinzmann S, Entian KD May 1996 "Biosynthesis of lantibiotic nisin Posttranslational modification of its prepeptide occurs at a multimeric membrane-associated lanthionine synthetase complex" J Biol Chem 271 21: 12294–301 doi:101074/jbc2712112294 PMID 8647829 
  10. ^ Goto, Y; Li, B; Claesen, J; Shi, Y; Bibb, MJ; van der Donk, WA 2010 "Discovery of unique lanthionine synthetases reveals new mechanistic and evolutionary insights" PLoS Biology 8 3: e1000339 doi:101371/journalpbio1000339 PMC 2843593  PMID 20351769 
  11. ^ Zhang, Q; Yu, Y; Vélasquez, JE; van der Donk, WA 2012 "Evolution of lanthipeptide synthetases" Proceedings of the National Academy of Sciences 109 45: 18361–6 doi:101073/pnas1210393109 PMC 3494888  PMID 23071302 
  12. ^ Brötz H, Sahl HG 2000 "New insights into the mechanism of action of lantibiotics—diverse biological effects by binding to the same molecular target" Journal of Antimicrobial Chemotherapy 46 1: 1–6 doi:101093/jac/4611 PMID 10882681 
  13. ^ Cotter, Hill, Ross 2005 "Bacterial Lantibiotics: Strategies to Improve Therapeutic Potential" PDF 6 Current Protein and Peptide Science: 61–75 CS1 maint: Multiple names: authors list link
  14. ^ a b van Kraaij C, de Vos WM, Siezen RJ, Kuipers OP October 1999 "Lantibiotics: biosynthesis, mode of action and applications" Nat Prod Rep 16 5: 575–87 doi:101039/a804531c PMID 10584332 
  15. ^ "New antibiotic compound enters phase I clinical trial" Press Release Wellcome Trust 2011-11-03 
  16. ^ Parker S 2012-08-06 "Novacta Biosystems Limited completes Phase I study of NVB302 against C difficile infection in healthy volunteers" Press Release Celtic Pharma Holding 
  17. ^ Hammami R, Zouhir A, Ben Hamida J, Fliss I 2007 "BACTIBASE: a new web-accessible database for bacteriocin characterization" BMC Microbiology 7: 89 doi:101186/1471-2180-7-89 PMC 2211298  PMID 17941971 
  18. ^ Hammami R, Zouhir A, Le Lay C, Ben Hamida J, Fliss I 2010 "BACTIBASE second release: a database and tool platform for bacteriocin characterization" BMC Microbiology 10: 22 doi:101186/1471-2180-10-22 PMC 2824694  PMID 20105292 
  19. ^ "Archived copy" Archived from the original on 2013-08-15 Retrieved 2013-07-25 

Further reading

  • Jack R, Bierbaum G, Heidrich C, Sahl HG September 1995 "The genetics of lantibiotic biosynthesis" BioEssays 17 9: 793–802 doi:101002/bies950170909 PMID 8763832 
  • Sahl HG, Jack RW, Bierbaum G June 1995 "Biosynthesis and biological activities of lantibiotics with unique post-translational modifications" Eur J Biochem 230 3: 827–53 doi:101111/j1432-103319950827gx PMID 7601145 
  • Sahl HG, Bierbaum G 1998 "Lantibiotics: biosynthesis and biological activities of uniquely modified peptides from gram-positive bacteria" Annu Rev Microbiol 52: 41–79 doi:101146/annurevmicro52141 PMID 9891793 
  • Stein T May 2005 "Bacillus subtilis antibiotics: structures, syntheses and specific functions" Mol Microbiol 56 4: 845–57 doi:101111/j1365-2958200504587x PMID 15853875 
  • Smith JL 2002 Structural and functional characterization of the lantibiotic mutacin PDF PhD University of Florida 

External links

  • "Complete list of lantibiotics" BACTIBASE Database 

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    Lantibiotics beatiful post thanks!


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