Bacteriocins

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Bacteriocins are proteinaceous toxins that are secreted by strains of bacteria and that inhibit the growth of other strains of the same or similar types of bacteria. It is estimated that 99% of all bacteria produce and excrete at least one bacteriocin. In contrast to the mostly low molecular weight antibiotics , bacteriocins are peptides or proteins . Your genetic information is encoded on plasmids . In contrast to the non-ribosomal peptides with similar effects as polymyxins and iturins , bacteriocins are produced on the ribosome .

Colicins were described as the first bacteriocins by André Gratia in Escherichia coli in 1925 .

Physiological role

Bacteriocins usually have a narrow spectrum of activity, especially to reduce nutrient competition, limited to species that are similar to the producer organism. Bacteriocins with broad spectrum activity are nisin from Lactococcus lactis and reutericyclin (from Lactobacillus reuteri ). Bacteriocins play a role in conquering and defending ecological niches against related bacterial strains. Bacteriocins also use bacteriocins as a competitive strategy for infectious diseases.

Classification of bacteriocins

Bacteriocins can be subdivided into different categories, for example according to the type of producer strain, the secretion, the spectrum of activity, the extent of the post-translational modification and according to the mode of action and resistance.

Bacteriocins from gram-positive bacteria are usually divided into one of the following four classes. Class I and II bacteriocins are relatively small, cationic , amphiphilic , biomembrane- binding peptides between three and ten kilodaltons . Class I bacteriocins contain the non-canonical amino acids lanthionine and methyllanthionine. Class II bacteriocins are further subdivided into three subtypes: IIa comprises peptides effective against Listeria with the N -terminal amino acid sequence YGNGVXCI, IIb heterodimeric bacteriocins, and IIc thiol -activated bacteriocins. Class III bacteriocins have a mass over 30 kilodaltons and are heat-labile . Class IV bacteriocins have lipids or glycosylations necessary for their function .

Bacteriocins from gram-negative bacteria are usually classified into three groups according to their size, but these also include genetic, structural and functional similarities. The microcines are peptides or small proteins up to a size of approx. 20 kDa. CLBs , from Colicin-like bacteriocins (German: Colicin-like bacteriocins), are between 20 and 90 kDa in size. Colicins are bacteriocins of the bacterium Escherichia coli . Similar bacteriocins are also found in other Gram negative bacteria. They can be further subdivided based on their cytotoxic mechanisms or based on their import mechanisms (groups A and B). Tailocins are large bacteriocins that consist of several subunits and resemble the tail structures of bacteriophages. The tailocins of Pseudomonas aeruginosa, which are further subdivided into F- and R-type pyocins , have been researched best .

Demarcation

Agrocin 84, a bacteriocin with broad spectrum activity from Agrobacterium radiobacter

Some other, mostly low-molecular-weight substances with antimicrobial properties, described as bacteriocins with broad-spectrum effects , such as Reuterin produced by Lactobacillus reuteri , do not belong to the bacteriocins in the narrower sense, since they are not cleaved by proteases and are therefore not peptides or proteins.

application

Some bacteriocins are of interest to the food industry. So you can nisin synthesized from lactic acid bacteria as a preservative in various products such as cheese spread use. The use of bacteriocins as antibiotics is under discussion.

Examples

  • Alveicin
  • Aureocin
  • Aureocin A53
  • Aureocin A70
  • Bisin
  • Carnocine
  • Carnocycline
  • Caseicin
  • Cerein
  • Circular in A
  • Colicins from coli bacteria ,
  • Curvaticin
  • Divercin
  • Duramycin from Streptomyces ,
  • Enterocin
  • Enterolysin
  • Epidermin / gallidermin
  • Erwiniocin
  • Gardimycin
  • Gassericin A [33]
  • Glycinecin
  • Halocin
  • Haloduracin
  • Lactocin S [34]
  • Lactococcin
  • Lacticin
  • Lantibiotics from various staphylococci containing lanthionine and methyllanthionine ,
  • Leucoccin
  • Lysostaphin
  • Macedocin
  • Mersacidin
  • Mesentericin
  • Microbisporicin
  • Microcin S.
  • Mutacin
  • Nisin from the lactic acid bacterium Lactococcus lactis .
  • Paenibacillin
  • Planosporicin
  • Pediocin
  • Pentocin
  • Plantaricin
  • Pneumocyclicin
  • Pyocine
  • Reutericin 6
  • Sakacin
  • Salivaricin
  • Sublancin
  • Subtle
  • Sulfolobicine
  • Syringacins 4-C and W-1 from Pseudomonas syringae pv. Syringae
  • Tasmancin
  • Thuricin 17
  • Trifolite toxin
  • Variacin
  • Vibriocin
  • Warnericin
  • Warning woman

See also

  • Eucaryocins - antimicrobial peptides and proteins synthesized by eukaryotes
  • Archaeocins - antimicrobial peptides and proteins synthesized by archaea

Individual evidence

  1. ↑ a b Institute for Medical Microbiology, Immunology and Parasitology: Bacteriocins - Lantibiotika ( Memento from November 11, 2013 in the Internet Archive ), University of Bonn .
  2. ^ A b Richard F. Shand, Kathryn J. Leyva: Archaeal Antimicrobials: An undiscovered country. In: Paul Blum (Ed.): Archaea: New Models for Prokaryotic Biology . Caister Academic Press, 2008, ISBN 978-1-904455-27-1 , pp. 233f.
  3. ↑ a b c d e f g H. Lee, HY Kim: Lantibiotics, class I bacteriocins from the genus Bacillus. In: Journal of microbiology and biotechnology. Volume 21, Number 3, March 2011, ISSN  1738-8872 , pp. 229-235. PMID 21464591 .
  4. ↑ A. Gratia: Sur un remarquable exemple d'antagonisme entre deux souches de colibacille. In: Compt. Rend. Soc. Biol. Volume 93, 1925, pp. 1040-1042.
  5. ↑ JP Gratia: Andre Gratia: a forerunner in microbial and viral genetics. In: Genetics. Volume 156, No. 2, 2000, pp. 471-6. PMID 11014798 . PMC 1461273 (free full text)
  6. ↑ Definition at UniProt
  7. ↑ KA Stevens et al: Nisin treatment for inactivation of Salmonella species and other gram-negative bacteria. In: Applied and Environmental Microbiology. Volume 57, No. 12, 1991, pp. 3613-3615.
  8. ^ E. Breukink, B. de Kruijff: The lantibiotic nisin, a special case or not? In: Biochimica et Biophysica Acta . Volume 1462, Numbers 1-2, December 1999, ISSN  0006-3002 , pp. 223-234. PMID 10590310 .
  9. ↑ Entry on Reutericyclin. In: Römpp Online . Georg Thieme Verlag, accessed on November 11, 2013.
  10. ↑ Kathryn E Holt et al: Tracking the Establishment of Local Endemic Populations of an Emergent Enteric Pathogen. In: Proceedings of the National Academy of Sciences . 110.43, 2013, pp. 17522-17527. doi: 10.1073 / pnas.1308632110 .
  11. ↑ Eric Cascales et al: Colicin Biology. In: Microbiology and Molecular Biology Reviews. 71.1, 2007, pp. 158-229. doi: 10.1128 / MMBR.00036-06 .
  12. ↑ Maarten GK Ghequire, René De Mot: Ribosomally Encoded Antibacterial Proteins and Peptides from Pseudomonas. In: FEMS Microbiology Reviews. 38.4, 2014, pp. 523-568. doi: 10.1111 / 1574-6976.12079
  13. ^ LT Axelsson, TC Chung, WJ Dobrogosz, SE Lindgren: Production of a Broad Spectrum Antimicrobial Substance by Lactobacillus reuteri. In: Microbial Ecology in Health and Disease. Vol. 2, No. 2, 1989, pp. 131-136. doi: 10.3109 / 08910608909140210 .
  14. ↑ Entry on Reuterin. In: Römpp Online . Georg Thieme Verlag, accessed on November 11, 2013.
  15. ↑ Manuel Montalbán-López et al: Are Bacteriocins Underexploited? NOVEL Applications for OLD Antimicrobials. In: Current Pharmaceutical Biotechnology. 12, 2011, pp. 1205-1220.
  16. ↑ P. Lavermiocca, SL Lonigro, F. Valerio, A. Evidente, A. Visconti: Reduction of Olive Knot Disease by a Bacteriocin from Pseudomonas syringae pv. Ciccaronei. In: Applied and environmental Microbiology. Vol 68, No. 3, 2002, pp. 1403-1407. PMC 123734 (free full text)

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