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Review
. 2013 Sep 30;11(10):3632-60.
doi: 10.3390/md11103632.

Antimicrobial peptides from marine proteobacteria

Florie Desriac  1 , Camille Jégou, Eric Balnois, Benjamin Brillet, Patrick Le Chevalier, Yannick Fleury
Affiliations
Review

Antimicrobial peptides from marine proteobacteria

Florie Desriac et al. Mar Drugs. .

Abstract

After years of inadequate use and the emergence of multidrug resistant (MDR) strains, the efficiency of "classical" antibiotics has decreased significantly. New drugs to fight MDR strains are urgently needed. Bacteria hold much promise as a source of unusual bioactive metabolites. However, the potential of marine bacteria, except for Actinomycetes and Cyanobacteria, has been largely underexplored. In the past two decades, the structures of several antimicrobial compounds have been elucidated in marine Proteobacteria. Of these compounds, polyketides (PKs), synthesised by condensation of malonyl-coenzyme A and/or acetyl-coenzyme A, and non-ribosomal peptides (NRPs), obtained through the linkage of (unusual) amino acids, have recently generated particular interest. NRPs are good examples of naturally modified peptides. Here, we review and compile the data on the antimicrobial peptides isolated from marine Proteobacteria, especially NRPs.

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Figures

Figure 1
Figure 1
Diagram of NRP biosynthesis. Aa: amino acid; A: adenylation domain; C: condensation domain; PCP: peptidyl carrier protein; and TE: thioesterase domain.
Figure 2
Figure 2
Structures of andrimid, moiramide B and their analogue 7.
Figure 3
Figure 3
The NRPS-PKS synthesis of andrimid [43]. KS: ketosynthase; DH: dehydratase; CLF: chain length factor; KR: ketoreductase; T: thiolation domain; TG: transglutaminase; A: adenylation domain; C: condensation domain; TE: thioesterase.
Figure 4
Figure 4
Structure of kahalalide F.
Figure 5
Figure 5
Biosynthesis of holomycin [31]. 3485: acyl-CoA dehydrogenase; 3486: thioesterase domain; 3489: phosphopantothenoylcysteine decarboxylase; 3487: glucose-mathanol-choline oxydoreductase; 3492: thioredoxin-disulphide reductase; 3483: acetyltransferase; Cy: cyclisation domain; A: adenylation domain; T: thiolation domain or peptidyl carrier protein (PCP).
Figure 6
Figure 6
Structures of unnarmicins, ngercheumicins and solonamides.
Figure 7
Figure 7
Structure of thiomarinols produced by Pseudoalteromonas sp. SANK 73390.
Figure 8
Figure 8
Structures of massetolides.
Figure 9
Figure 9
Antibiotic peptides from Myxococcus fulvus.
Figure 10
Figure 10
Antifungal peptides from Paraliomyxa miuraensis.
Figure 11
Figure 11
Jaspamide-related cyclic depsipeptides.
Figure 12
Figure 12
NRPS-PKS biosynthesis of the chondramides [103]. ACP: acyl carrier protein; KS: ketosynthase; AT: acyl transferase; DH: β-hydroxy dehydratase; KR: β-ketoacyl reductase; ER: enoyl reductase; C: condensation domain; A: adenylation domain; MT: methyltransferase domain; PCP: peptidyl carrier protein; E: epimerisation domain; TE: thioesterase domain; PEP: phosphoenolpyruvate domain.
Figure 13
Figure 13
Cyclic peptides microsclerodermin D and pedein A.
Figure 14
Figure 14
Saframycin-related peptides.
See this image and copyright information in PMC

References

    1. Singh S.B., Barrett J.F. Empirical antibacterial drug discovery-foundation in natural products. Biochem. Pharmacol. 2006;71:1006–1015. doi: 10.1016/j.bcp.2005.12.016. - DOI - PubMed
    1. Joint I., Mühling M., Querellou J. Culturing marine bacteria—An essential prerequisite for biodiscovery. Microb. Biotechnol. 2010;3:564–575. doi: 10.1111/j.1751-7915.2010.00188.x. - DOI - PMC - PubMed
    1. Fortman J.L., Sherman D.H. Utilizing the power of microbial genetics to bridge the gap between the promise and the application of marine natural products. Chembiochem. 2005;6:960–978. doi: 10.1002/cbic.200400428. - DOI - PubMed
    1. Giovannoni S., Stingl U. The importance of culturing bacterioplankton in the “omics” age. Nat. Rev. Microbiol. 2007;5:820–826. doi: 10.1038/nrmicro1752. - DOI - PubMed
    1. King G.M., Smith C.B., Tolar B., Hollibaugh J.T. Analysis of composition and structure of coastal to mesopelagic bacterioplankton communities in the northern gulf of Mexico. Front. Microbiol. 2012;3:438–451. - PMC - PubMed

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