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@ARTICLE{Pashou:1006811,
      author       = {Pashou, Efthimia and Reich, Sebastian J. and Reiter,
                      Alexander and Weixler, Dominik and Eikmanns, Bernhard J. and
                      Oldiges, Marco and Riedel, Christian U. and Goldbeck,
                      Oliver},
      title        = {{I}dentification and {C}haracterization of {C}orynaridin, a
                      {N}ovel {L}inaridin from {C}orynebacterium lactis},
      journal      = {Microbiology spectrum},
      volume       = {11},
      number       = {1},
      issn         = {2165-0497},
      address      = {Birmingham, Ala.},
      publisher    = {ASM},
      reportid     = {FZJ-2023-01864},
      pages        = {e01756-22},
      year         = {2023},
      abstract     = {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.},
      cin          = {IBG-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBG-1-20101118},
      pnm          = {2171 - Biological and environmental resources for
                      sustainable use (POF4-217)},
      pid          = {G:(DE-HGF)POF4-2171},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36541778},
      UT           = {WOS:000899411900001},
      doi          = {10.1128/spectrum.01756-22},
      url          = {https://juser.fz-juelich.de/record/1006811},
}