Purification and characterization of cytolysins from Listeria monocytogenes serovar 4b and Listeria ivanovii.
Year: 1989
Type: article
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 O (SLO), and this protein has therefore been termed listeriolysin O (LLO). In addition a protein of Mr 24 kDa from culture supernatants of L. ivanovii co-purified with LLO. The N-terminal aminoacid sequences of both proteins from L. ivanovii have been determined. By mutagenesis with transposons of Gram-positive origin (Tn916 and Tn1545), 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 mutants will be presented.
Source: PubMed
Authors: J Kreft, D Funke, R Schlesinger, F Lottspeich, W Goebel
Institution: University of Würzburg
Language: English
Subfield: Food Science
Domain: Life Sciences
Open Access status: green
Funder: Deutsche Forschungsgemeinschaft
Award: G5039202075
OpenAlex ID: W2187629324