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  - 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  - 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  - Gilmore, Michael S.
A1  - Cruz-Rodz, Armando L.
A1  - Leimeister-Wächter, Michaela
A1  - Kreft, Jürgen
A1  - Goebel, Werner
T1  - A Bacillus cereus cytolytic determinant, cereolysin AB, which comprises the phospholipase C and sphingomyelinase genes: nucleotide sequence and genetic linkage
N2  - A cloned cytolytic determinant from the genome of Bacillus cereus GP-4 has been characterized at the molecular Ievel. Nucleotide sequence determination revealed the presence of two open reading frames. 8oth open reading frames were found by deletion and complementation analysis to be necessary for expression of the hemolytic phenotype by Bacillus subtilis and Escherichia coli hosts. The 5' open reading frame was found to be nearly identical to a recently reported phospholipase C gene derived from a mutant B. cereus strain which overexpresses the respective protein, and it conferred a lecithinase-positive phenotype to the B. subtilis host. The 3' open reading frame encoded a sphingomyelinase. The two tandemly encoded activities, phospholipase C and sphingomyelinase, constitute a biologically functional cytolytic determinant of B. cereus termed cereolysin AB.
KW  - Biologie
Y1  - 1989
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-60588
ER  -