Kreft J, Funke D, Haas A, Lottspeich F, Goebel W
Institut für Genetik und Mikrobiologie, University of Würzburg, F.R.G.
FEMS Microbiol Lett. 1989 Jan 15;48(2):197-202. doi: 10.1111/j.1574-6968.1989.tb03298.x.
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.
在伊氏李斯特菌和单核细胞增生李斯特菌Sv4b的培养上清液中,首次鉴定出一种分子量为58 kDa的溶血素,它具有SH激活的细胞溶素的所有特征,因此被鉴定为李斯特菌溶血素O(LLO)。就伊氏李斯特菌而言,一种分子量为24 kDa的第二主要上清液蛋白与LLO共纯化。然而,这种蛋白质的功能有待确定。在伊氏李斯特菌的培养上清液中可检测到鞘磷脂酶和卵磷脂酶活性,这两种酶活性共同导致了伊氏李斯特菌引起的明显溶血。文中展示了伊氏李斯特菌LLO和24 kDa蛋白的N端氨基酸序列。