TY - JOUR
A1 - Härtlein, Michael
A1 - Schiessl, Sigrid
A1 - Wagner, Wilma
A1 - Rdest, Ursula
A1 - Kreft, Jürgen
A1 - Goebel, Werner
T1 - Transport of hemolysin by Escherichia coli
N2 - No abstract available
KW - Biologie
KW - Hemolysin
KW - Escberichia coli
KW - Gene cloning
KW - Expression
KW - Transport
Y1 - 1983
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60619
ER -
TY - JOUR
A1 - Lampidis, Robert
A1 - Gross, Roy
A1 - Sokolovic, Zeljka
A1 - Goebel, Werner
A1 - Kreft, Jürgen
T1 - 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
N2 - No abstract available
KW - Biologie
Y1 - 1994
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60503
ER -
TY - JOUR
A1 - Kreft, Jürgen
A1 - Bernhard, K.
A1 - Goebel, Werner
T1 - Recombinant plasmids capable to replication in B. subtilis and E. coli
N2 - The plasmid pBC16 (4.25 kbases), ongtnally isolated from Bacillus cereus, determines tetracycline resistance and can be transformed into competent cells of B. subtilis. A miniplasmid of pBCl6 (pBCI6-1), 2,7 kb) which has lost an EcoRI fragment of pBCI6 retains the replication functions and the tetracycline resistance. This plasmid which carries only one EcoRI site has been joined in vitro to pBS], a cryptic plasmid previously isolated from B. subtilis and shown to carry also a single EcoRI site (Bernhard et aI., 1978). The recombinant plasmid is unstable and dissociates into the plasmid pBSl61 (8.2 kb) and the smaller plasmid pBS162 (2. I kb). Plasmid pBS161 retains the tetracycline resistance. It possesses a single EcoRI site and 6 HindlII sites. The largest HindIII fragment of pBS161 carries the tetracycline resistance gene and the replication function. After circularization in vitro of this fragment a new plasmid, pBS161-l is generated, which can be used as a HindlII and EcoRI cloning vector in Bacillus suhtilis. Hybrid plasmids consisting of the E. coli plasmids pBR322, p WL 7 or pACl84 and different HindlII fragments of pBSI61 were constructed in vitro. Hybrids containing together with the E. coli plasmid the largest HindlII fragment of pBS161 can replicate in E. coli and B. sublilis. In E. coli only the replicon of the E. coli plasmid part is functioning whereas in B. suhtilis replication of the hybrid plasmid is under the control of the Bacillus replicon. The tetracycline resistance of the B. subtilis plasmid is expressed in E. coli, but several antibiotic resistances of the E. coli plasmids (ampicillin, kanamycin and chloramphenicol) are not expressed in B. suhtilis. The hybrid plasmids seem to be more unstable in B. subtilis than in E. coli.
Y1 - 1978
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-47000
ER -
TY - JOUR
A1 - Kreft, Jürgen
A1 - Funke, D.
A1 - Schlesinger, R.
A1 - Lottspeich, F.
A1 - Goebel, Werner
T1 - Purification and characterization of cytolysins from Listeria monocytogenes serovar 4b and Listeria ivanovii
N2 - 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.
Y1 - 1989
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-47036
ER -
TY - JOUR
A1 - Kreft, Jürgen
A1 - Funke, Dorothee
A1 - Haas, Albert
A1 - Lottspeich, Friedrich
A1 - Goebel, Werner
T1 - Production, purification and characterization of hemolysins from Listeria ivanovii and Listeria monocytogenes Sv4b.
N2 - 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.
KW - Biologie
KW - Hemolysin
KW - Listeria
Y1 - 1989
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60545
ER -
TY - JOUR
A1 - Schülein, Ralf
A1 - Kreft, Jürgen
A1 - Gonski, Sigrid
A1 - Goebel, Werner
T1 - Preprosubtilisin Carlsberg processing and secretion is blocked after deletion of amino acids 97-101 in the mature part of the enzyme
N2 - 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, Mr=42 kDa) was not processed to the mature form (Mr = 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, Mr = 38 kDa) oftbis protease could be demonstrated. P38c very probably represents a genuine proform of subtilisin Carlsberg.
KW - Biologie
KW - Bacillus
KW - Proenzyme
KW - Subtilisin maturation
KW - Site-directed mutagenesis
KW - Subtilisin Carlsberg
Y1 - 1991
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60577
ER -
TY - JOUR
A1 - Eisenreich, Wolfgang
A1 - Rudel, Thomas
A1 - Heesemann, Jürgen
A1 - Goebel, Werner
T1 - Persistence of Intracellular Bacterial Pathogens—With a Focus on the Metabolic Perspective
JF - Frontiers in Cellular and Infection Microbiology
N2 - Persistence has evolved as a potent survival strategy to overcome adverse environmental conditions. This capability is common to almost all bacteria, including all human bacterial pathogens and likely connected to chronic infections caused by some of these pathogens. Although the majority of a bacterial cell population will be killed by the particular stressors, like antibiotics, oxygen and nitrogen radicals, nutrient starvation and others, a varying subpopulation (termed persisters) will withstand the stress situation and will be able to revive once the stress is removed. Several factors and pathways have been identified in the past that apparently favor the formation of persistence, such as various toxin/antitoxin modules or stringent response together with the alarmone (p)ppGpp. However, persistence can occur stochastically in few cells even of stress-free bacterial populations. Growth of these cells could then be induced by the stress conditions. In this review, we focus on the persister formation of human intracellular bacterial pathogens, some of which belong to the most successful persister producers but lack some or even all of the assumed persistence-triggering factors and pathways. We propose a mechanism for the persister formation of these bacterial pathogens which is based on their specific intracellular bipartite metabolism. We postulate that this mode of metabolism ultimately leads, under certain starvation conditions, to the stalling of DNA replication initiation which may be causative for the persister state.
KW - persistence
KW - mechanisms of persister formation
KW - intracellular bacterial pathogens
KW - stress conditions
KW - ATP-DnaA complex
KW - DNA replication initiation
Y1 - 2021
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-222348
SN - 2235-2988
VL - 10
ER -
TY - JOUR
A1 - Kreft, Jürgen
A1 - Haas, Albert
A1 - Goebel, Werner
T1 - Isolation and characterization of genes coding for proteins involved in the cytolysis by Listeria ivanovii
N2 - 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.
Y1 - 1989
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-46991
ER -
TY - JOUR
A1 - Eisenreich, Wolfgang
A1 - Rudel, Thomas
A1 - Heesemann, Jürgen
A1 - Goebel, Werner
T1 - How viral and intracellular bacterial pathogens reprogram the metabolism of host cells to allow their intracellular replication
JF - Frontiers in Cellular and Infection Microbiology
N2 - Viruses and intracellular bacterial pathogens (IBPs) have in common the need of suitable host cells for efficient replication and proliferation during infection. In human infections, the cell types which both groups of pathogens are using as hosts are indeed quite similar and include phagocytic immune cells, especially monocytes/macrophages (MOs/MPs) and dendritic cells (DCs), as well as nonprofessional phagocytes, like epithelial cells, fibroblasts and endothelial cells. These terminally differentiated cells are normally in a metabolically quiescent state when they are encountered by these pathogens during infection. This metabolic state of the host cells does not meet the extensive need for nutrients required for efficient intracellular replication of viruses and especially IBPs which, in contrast to the viral pathogens, have to perform their own specific intracellular metabolism to survive and efficiently replicate in their host cell niches. For this goal, viruses and IBPs have to reprogram the host cell metabolism in a pathogen-specific manner to increase the supply of nutrients, energy, and metabolites which have to be provided to the pathogen to allow its replication. In viral infections, this appears to be often achieved by the interaction of specific viral factors with central metabolic regulators, including oncogenes and tumor suppressors, or by the introduction of virus-specific oncogenes. Less is so far known on the mechanisms leading to metabolic reprogramming of the host cell by IBPs. However, the still scant data suggest that similar mechanisms may also determine the reprogramming of the host cell metabolism in IBP infections. In this review, we summarize and compare the present knowledge on this important, yet still poorly understood aspect of pathogenesis of human viral and especially IBP infections.
KW - metabolic adaptation
KW - viruses
KW - intracellular bacterial pathogens
KW - metabolism of infected and uninfected host cells
KW - reprogamming of host cell metabolism
Y1 - 2019
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-197188
SN - 2235-2988
VL - 9
ER -
TY - JOUR
A1 - Goebel, Werner
A1 - Kathariou, S.
A1 - Kuhn, M.
A1 - Sokolovic, Z.
A1 - Kreft, Jürgen
A1 - Köhler, S.
A1 - Funke, D.
A1 - Chakraborty, T.
A1 - Leimeister-Wächter, M.
T1 - Hemolysin from Listeria-biochemistry, genetics and function in pathogenesis
N2 - No abstract available
KW - Biologie
Y1 - 1988
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60563
ER -