@article{OndruschKreft2011,
  author    = {Ondrusch, Nicolai and Kreft, J{\"u}rgen},
  title     = {Blue and Red Light Modulates SigB-Dependent Gene Transcription, Swimming Motility and Invasiveness in Listeria monocytogenes},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-75451},
  year      = {2011},
  abstract  = {Background: In a number of gram-positive bacteria, including Listeria, the general stress response is regulated by the alternative sigma factor B (SigB). Common stressors which lead to the activation of SigB and the SigB-dependent regulon are high osmolarity, acid and several more. Recently is has been shown that also blue and red light activates SigB in Bacillus subtilis. Methodology/Principal Findings: By qRT-PCR we analyzed the transcriptional response of the pathogen L. monocytogenes to blue and red light in wild type bacteria and in isogenic deletion mutants for the putative blue-light receptor Lmo0799 and the stress sigma factor SigB. It was found that both blue (455 nm) and red (625 nm) light induced the transcription of sigB and SigB-dependent genes, this induction was completely abolished in the SigB mutant. The blue-light effect was largely dependent on Lmo0799, proving that this protein is a genuine blue-light receptor. The deletion of lmo0799 enhanced the red-light effect, the underlying mechanism as well as that of SigB activation by red light remains unknown. Blue light led to an increased transcription of the internalin A/B genes and of bacterial invasiveness for Caco-2 enterocytes. Exposure to blue light also strongly inhibited swimming motility of the bacteria in a Lmo0799- and SigB-dependent manner, red light had no effect there. Conclusions/Significance: Our data established that visible, in particular blue light is an important environmental signal with an impact on gene expression and physiology of the non-phototrophic bacterium L. monocytogenes. In natural environments these effects will result in sometimes random but potentially also cyclic fluctuations of gene activity, depending on the light conditions prevailing in the respective habitat.},
  subject      = {Listeria monocytogenes},
  language  = {en}
}
@article{OndruschKreft2011,
  author    = {Ondrusch, Nicolai and Kreft, J{\"u}rgen},
  title     = {Blue and Red Light Modulates SigB-Dependent Gene Transcription, Swimming Motility and Invasiveness in \(Listeria\) \(monocytogenes\)},
  series = {PLoS ONE},
  volume    = {6},
  journal   = {PLoS ONE},
  number    = {1},
  doi       = {10.1371/journal.pone.0016151},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-134050},
  pages     = {e16151},
  year      = {2011},
  abstract  = {Background: In a number of gram-positive bacteria, including Listeria, the general stress response is regulated by the alternative sigma factor B (SigB). Common stressors which lead to the activation of SigB and the SigB-dependent regulon are high osmolarity, acid and several more. Recently is has been shown that also blue and red light activates SigB in Bacillus subtilis. Methodology/Principal Findings: By qRT-PCR we analyzed the transcriptional response of the pathogen L. monocytogenes to blue and red light in wild type bacteria and in isogenic deletion mutants for the putative blue-light receptor Lmo0799 and the stress sigma factor SigB. It was found that both blue (455 nm) and red (625 nm) light induced the transcription of sigB and SigB-dependent genes, this induction was completely abolished in the SigB mutant. The blue-light effect was largely dependent on Lmo0799, proving that this protein is a genuine blue-light receptor. The deletion of lmo0799 enhanced the red-light effect, the underlying mechanism as well as that of SigB activation by red light remains unknown. Blue light led to an increased transcription of the internalin A/B genes and of bacterial invasiveness for Caco-2 enterocytes. Exposure to blue light also strongly inhibited swimming motility of the bacteria in a Lmo0799- and SigB-dependent manner, red light had no effect there. Conclusions/Significance: Our data established that visible, in particular blue light is an important environmental signal with an impact on gene expression and physiology of the non-phototrophic bacterium L. monocytogenes. In natural environments these effects will result in sometimes random but potentially also cyclic fluctuations of gene activity, depending on the light conditions prevailing in the respective habitat.},
  language  = {en}
}
@article{LampidisGrossSokolovicetal.1994,
  author    = {Lampidis, Robert and Gross, Roy and Sokolovic, Zeljka and Goebel, Werner and Kreft, J{\"u}rgen},
  title     = {The virulence regulator protein of Listeria ivanovii is highly homologous to PrfA from Listeria monocytogenes and both belong to the Crp-Fnr family of transcription regulators},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-60503},
  year      = {1994},
  abstract  = {No abstract available},
  subject      = {Biologie},
  language  = {en}
}
@article{BrehmHaasGoebeletal.1992,
  author    = {Brehm, Klaus and Haas, Albert and Goebel, Werner and Kreft, J{\"u}rgen},
  title     = {A gene encoding a superoxide dismutase of the facultative intracellular bacterium Listeria monocytogenes},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-60515},
  year      = {1992},
  abstract  = {A gene (Imsod) encoding superoxide dismutase (SOD; EC 1.15.1.1) of the facultative intracellular pathogen, Listeria monocytogenes, was cloned by functional complementation of an SOD-deficient Escherichia coli mutant. The nucleotide sequence was determined and the deduced amino acid (aa) sequence (202 aa) showed close similarity to manganese-containing SOD's from other organisms. Subunits of the recombinant L. monocytogenes SOD (re-SOD) and of both E. coli SODs formed enzymatically active hybrid enzymes in vivo. DNA/DNA-hybridization experiments showed that this type of recombinant re-sod gene is conserved within the genus Listeria.},
  subject      = {Biologie},
  language  = {en}
}
@article{HaasDumbskyKreft1992,
  author    = {Haas, Albert and Dumbsky, Martina and Kreft, J{\"u}rgen},
  title     = {Listeriolysin genes: complete sequence of ilo from Listeria ivanovii and of lso from Listeria seeligeri},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-60529},
  year      = {1992},
  abstract  = {The completc DNA scqucnccs coding for thc thiol-activated cytolysins from Listeria ivanovii, ivanolysin 0 (ILO) and for sccligerolysin 0 (LSO) from Listeria seeligeri have been dctermined. Thc deduced amino acid scquences revealed that: (i) the primary translation products comprise 528 (ILO) and 530 (LSO) amino acids. respectively. (ii) ILO contains two cysteines. LSO has a substitution in the conserved cysteine motif.},
  subject      = {Biologie},
  language  = {en}
}
@article{HaasBrehmKreftetal.1991,
  author    = {Haas, Albert and Brehm, Klaus and Kreft, J{\"u}rgen and Goebel, Werner},
  title     = {Cloning, characterization, and expression in Escherichia coli of a gene encoding Listeria seeligeri catalase, a bacterial enzyme highly homologous to mammalian catalases},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-60536},
  year      = {1991},
  abstract  = {A gene coding for catalase (hydrogen-peroxide:hydrogen-peroxide oxidoreductase; EC 1.11.1.6) of the grain-positive bacterium Listeria seeligeri was cloned from a plasmid library of EcoRI-digested chromosomal DNA, with Escherichia coli DHSa as a host. The recombinant catalase was expressed in E. coli to an enzymatic activity approximately SO times that of the combined E. coli catalases. The nucleutide sequence was determined, and the deduced amino acid sequence revealed 43.2\% amino acid sequence identity between bovine liver catalase and L. seeligeri catalase. Most of the amino acid residues which are involved in catalytic activity, the formation of the active center accession channel, and heme binding in bovine liver catalase were also present in L. seeligeri catalase at the corresponding positions. The recombinant protein contained 488 amino acid residues and had a calculated molecular weight of 55,869. The predicted isoelectric point was 5.0. Enzymatic and genetic analyses showed that there is most probably a single catalase of this type in L. seeligeri. A perfect 21-bp inverted repeat, which was highly homologous to previously reported binding sequences of the Fur (ferric uptake regulon) protein of E. coli, was detected next to the putative promoter region of tbe L. seeligeri catalase gene.},
  subject      = {Biologie},
  language  = {en}
}
@article{SchueleinKreftGonskietal.1991,
  author    = {Sch{\"u}lein, Ralf and Kreft, J{\"u}rgen and Gonski, Sigrid and Goebel, Werner},
  title     = {Preprosubtilisin Carlsberg processing and secretion is blocked after deletion of amino acids 97-101 in the mature part of the enzyme},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-60577},
  year      = {1991},
  abstract  = {During an investigation into the substrate specificity and processing of subtilisin Carlsberg from Bacillus licheniformis, two major independent findings were made: (i) as has been shown previously, a stretch of five amino acids (residues 97-101 of the mature enzyme) that loops out into the binding cleft is involved in substrate binding by subtilisin Carlsberg. In order to see whether this loop element also determines substrate specificity, the coding region for these five amino acids was deleted from the cloned gene for subtilisin Carlsberg by site-directed mutagenesis. Unexpectedly the resulting mutant preproenzyme (P42c, M<sub>r</sub>=42 kDa) was not processed to the mature form (M<sub>r</sub> = 30 kDa) and was not released into the medium by a proteasedeficient B. subtilis host strain; rather, it accumulated in the cell membrane. This result demonstrates that the integrity of this loop element, which is very distant from the processing cleavage sites in the preproenzyme, is required for secretion of subtilisin Carlsberg. (ii) In culture supernatants from B. subtilis harbouring the cloned wild-type subtilisin Carlsberg gene the transient appearance (at 0-3 h after onset of stationary phase) of a processing intermediate (P38c, M<sub>r</sub> = 38 kDa) oftbis protease could be demonstrated. P38c very probably represents a genuine proform of subtilisin Carlsberg.},
  subject      = {Biologie},
  language  = {en}
}
@article{KreftFunkeSchlesingeretal.1989,
  author    = {Kreft, J{\"u}rgen and Funke, D. and Schlesinger, R. and Lottspeich, F. and Goebel, Werner},
  title     = {Purification and characterization of cytolysins from Listeria monocytogenes serovar 4b and Listeria ivanovii},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-47036},
  year      = {1989},
  abstract  = {Several exoproteins from Listeria monocytogenes serovar 4b (NCTC 10527) and Listeria ivanovii (ATCC) 19119, SLCC 2379), respectively, have been purified to homogeneity by thiol-disulfide exchange chromatography and gel filtration. Both strains produce a haemolytic/cytolytic protein of Mr 58 kDa, which has all the properties of a SH-activated cytolysin, the prototype of which is streptolysin 0 (SLO), and this protein has therefore heen termed Iisteriolysin 0 (LLO). In addition a protein of Mr 24 kDa from culture supernatants of L. ivanovii co-purified withLLO. The N-terminal aminoacid sequences of both proteins from L. ivanovii have been determined. By mutagenesis with transposons of Gram-positive origin (Tn916 and TnI545), which have been introduced via conjugation into L. ivanovii, several phenotypic mutants (altered haemolysis on sheep blood agar or lecithinase-negative) were obtained. Results on the properties of these muntants will he presented.},
  language  = {en}
}
@article{KreftHaasGoebel1989,
  author    = {Kreft, J{\"u}rgen and Haas, Albert and Goebel, Werner},
  title     = {Isolation and characterization of genes coding for proteins involved in the cytolysis by Listeria ivanovii},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-46991},
  year      = {1989},
  abstract  = {We established a library of chromosomal DNA of Listeria ivanovii in the pTZ19R plasmid system, using Escherichia coli DH5alpha as the host. One recombinant clone reacted strongly with a polyclonal antiserum raised against the listeriolysin 0 and a second exoprotein (24kDa) of L. ivanovii, which is most probably also involved in cytolytic processes. The recombinant E. coli clone may contain part of the listeriolysin 0 gene of L. ivanovii.},
  language  = {en}
}
@article{KreftFunkeHaasetal.1989,
  author    = {Kreft, J{\"u}rgen and Funke, Dorothee and Haas, Albert and Lottspeich, Friedrich and Goebel, Werner},
  title     = {Production, purification and characterization of hemolysins from Listeria ivanovii and Listeria monocytogenes Sv4b.},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-60545},
  year      = {1989},
  abstract  = {In culture supematants of both Listeria ivanovii and Listeria monocytogenes Sv4b, for the first time a hemolysin of molecular weight 58 kDa was identified, which had all the characteristics of an SH-activated cytolysin, and which was therefore identified as Iisteriolysin 0 (LLO). In the case of L. ivanovii a second major supematant protein of molecular weight 24 kDa co-purified with LLO. However, the function of this protein has to be determined. In culture supematants of L. ivanovii a sphingomyelinase and a Iecithinase activity could be detected, both enzymatic activities together contributing to the pronounced hemolysis caused by L. ivanovii. The N-tenninal amino acid sequences of LLO and the 24 kDa from L. ivanovii are shown.},
  subject      = {Biologie},
  language  = {en}
}