Hauptseite > Publikationsdatenbank > Identification and Characterization of Corynaridin, a Novel Linaridin from Corynebacterium lactis > print |
001 | 1006811 | ||
005 | 20231027114401.0 | ||
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037 | _ | _ | |a FZJ-2023-01864 |
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100 | 1 | _ | |a Pashou, Efthimia |0 P:(DE-HGF)0 |b 0 |
245 | _ | _ | |a Identification and Characterization of Corynaridin, a Novel Linaridin from Corynebacterium lactis |
260 | _ | _ | |a Birmingham, Ala. |c 2023 |b ASM |
336 | 7 | _ | |a article |2 DRIVER |
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520 | _ | _ | |a Genome analysis of Corynebacterium lactis revealed a bacteriocin gene cluster encoding a putative bacteriocin of the linaridin family of ribosomally synthesized and posttranslationally modified peptides (RiPPs). The locus harbors typical linaridin modification enzymes but lacks genes for a decarboxylase and methyltransferase, which is unusual for type B linaridins. Supernatants of Corynebacterium lactis RW3-42 showed antimicrobial activity against Corynebacterium glutamicum. Deletion of the precursor gene crdA clearly linked the antimicrobial activity of the producer strain to the identified gene cluster. Following purification, we observed potent activity of the peptide against Actinobacteria, mainly other members of the genus Corynebacterium, including the pathogenic species Corynebacterium striatum and Corynebacterium amycolatum. Also, low activity against some Firmicutes was observed, but there was no activity against Gram-negative species. The peptide is resilient towards heat but sensitive to proteolytic degradation by trypsin and proteinase K. Analysis by mass spectrometry indicates that corynaridin is processed by cleaving off the leader sequence at a conserved motif and posttranslationally modified by dehydration of all threonine and serin residues, resulting in a monoisotopic mass of 3,961.19 Da. Notably, time-kill kinetics and experiments using live biosensors to monitor membrane integrity suggest bactericidal activity that does not involve formation of pores in the cytoplasmic membrane. As Corynebacterium species are ubiquitous in nature and include important commensals and pathogens of mammalian organisms, secretion of bacteriocins by species of this genus could be a hitherto neglected trait with high relevance for intra- and interspecies competition and infection. |
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588 | _ | _ | |a Dataset connected to CrossRef, Journals: juser.fz-juelich.de |
700 | 1 | _ | |a Reich, Sebastian J. |b 1 |
700 | 1 | _ | |a Reiter, Alexander |0 P:(DE-Juel1)176811 |b 2 |
700 | 1 | _ | |a Weixler, Dominik |0 P:(DE-HGF)0 |b 3 |
700 | 1 | _ | |a Eikmanns, Bernhard J. |0 P:(DE-HGF)0 |b 4 |
700 | 1 | _ | |a Oldiges, Marco |0 P:(DE-Juel1)129053 |b 5 |
700 | 1 | _ | |a Riedel, Christian U. |0 0000-0001-7134-7085 |b 6 |
700 | 1 | _ | |a Goldbeck, Oliver |0 P:(DE-HGF)0 |b 7 |e Corresponding author |
773 | _ | _ | |a 10.1128/spectrum.01756-22 |g Vol. 11, no. 1, p. e01756-22 |0 PERI:(DE-600)2807133-5 |n 1 |p e01756-22 |t Microbiology spectrum |v 11 |y 2023 |x 2165-0497 |
856 | 4 | _ | |u https://juser.fz-juelich.de/record/1006811/files/spectrum.01756-22.pdf |y OpenAccess |
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