Lantibiotics

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Gallidermin
Identifiers
SymbolGallidermin
TCDB
1.C.20
OPM superfamily161
OPM protein1mqy
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Lantibiotics are a class of poly

amino acids lanthionine or methyllanthionine, as well as the unsaturated amino acids dehydroalanine, and 2-aminoisobutyric acid. They belong to ribosomally synthesized and post-translationally modified peptides
.

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

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.

phosphoethanolamine in the membranes
of its target cells and seem to disrupt several physiological functions.

History

The name lantibiotics was introduced in 1988 as an abbreviation for "lanthionine-containing peptide antibiotics".

bacterial resistance. These attributes of lantibiotics have led to more detailed research into their structures and biosynthetic pathways
.

Classification

Some contain 2 peptides, e.g. haloduracin.[6]

Examples

Lantibiotic Type # of
residues		 # of
thioether links		 Other
links[clarification needed]		 refs
nisin
subtilin		 A 34 5 0
gallidermin
epidermin		 A 21 3 1 [2]
mersacidin B 20 4 [3]
actagardine B 19 4 0
cinnamycin
duramycin		 B 19 3 1 [5]
sublancin 168 ? 37 1 2 [7]
plantaricin C B 27 4 0

(Sublancin may be an S-linked glycopeptide).[8]

Biosynthesis

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.[9] There are four known enzymes (lanthipeptide synthetases) responsible for producing lanthionine rings.[10][11]

Mechanism of action

Lantibiotics show substantial specificity for some components (e.g.,

cell membranes especially of Gram-positive bacteria. Type A lantibiotics kill rapidly by pore formation, type B lantibiotics inhibit peptidoglycan biosynthesis.[12] They are active in very low concentrations.[13]

Application

Food preservation

Lantibiotics are produced by Gram-positive bacteria and show strong antimicrobial action toward a wide range of other Gram-positive bacteria.

pathogens that cause food spoilage) and the pharmaceutical industry (to prevent or fight infections in humans or animals).[14]

Clinical antibiotic

One type known as B lantibiotic

Clostridium difficile,[15] and reported good results in 2012.[16]

Databases

BACTIBASE is an open-access database for bacteriocins including lantibiotics.[17][18] LANTIBASE is a lantibiotic specific resource.[19]

References

  1. PMID 15700960
    .
  2. ^
    PMID 3181159
    .
  3. ^
    PMID 18947397
    .
  4. PMID 7793878
    .
  5. ^
    PMID 12446685
    .
  6. PMID 18940665
    .
  7. S2CID 20144405
    .
  8. PMID 21196935
    .
  9. PMID 8647829
    .
  10. PMID 20351769
    .
  11. PMID 23071302
    .
  12. PMID 10882681
    .
  13. PMID 15638769. Archived from the original (PDF) on 2007-09-28. Retrieved 2007-06-01.{{cite journal}}: CS1 maint: multiple names: authors list (link
    )
  14. ^
    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. Archived from the original on 2013-09-01. Retrieved 2013-03-23.
  17. PMID 17941971
    .
  18. PMID 20105292
    .
  19. ^ "DBT Centre for Bioinformatics Presidency University, Kolkata". Archived from the original on 2013-08-15. Retrieved 2013-07-25.

Further reading

External links

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