Production, purification and characterization of hemolysins from Listeria ivanovii and Listeria monocytogenes Sv4b.
In culture supernatants 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 listeriolysin O (LLO). In the case of L. ivanovii a second major supernatant protein of molecular weight 24 kDa co-purified with LLO. However, the function of this protein has to be determined. In culture supernatants of L. ivanovii a sphingomyelinase and a lecithinase activity could be detected, both enzymatic activities together contributing to the pronounced hemolysis caused by L. ivanovii. The N-terminal amino acid sequences of LLO and the 24 kDa from L. ivanovii are shown.
Kreft
J
J
Institut für Genetik und Mikrobiologie, University of Würzburg, F.R.G.
Funke
D
D
Haas
A
A
Lottspeich
F
F
Goebel
W
W
D000595:Amino Acid Sequence; D001427:Bacterial Toxins; D006360:Heat-Shock Proteins / Q000302:isolation & purification; D006460:Hemolysin Proteins / Q000096:biosynthesis* / Q000302:isolation & purification / Q000502:physiology; D008087:Listeria / Q000276:immunology* / Q000472:pathogenicity; D008089:Listeria monocytogenes / Q000276:immunology / Q000472:pathogenicity; D008969:Molecular Sequence Data; D008970:Molecular Weight; D014774:Virulence
D001427:Bacterial Toxins; D006360:Heat-Shock Proteins; D006460:Hemolysin Proteins; C038705:hlyA protein, Listeria monocytogenes