Seeligeriolysin O, a cholesterol-dependent cytolysin of Listeria seeligeri, induces gamma interferon from spleen cells of mice

Seeligeriolysin O, a cholesterol-dependent cytolysin of Listeria seeligeri, induces gamma interferon from spleen cells of mice
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DOI:
10.1128/iai.71.1.234-241.2003
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发表时间:
2003-01-01
影响因子:
3.1
通讯作者:
Mitsuyama, M
Mitsuyama, M
中科院分区:
医学2区
文献类型:
--
作者:
Ito, Y;Kawamura, I;Mitsuyama, M

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Seeligeriolysin O(LSO)是由李斯特菌(Listeria seeligeri)产生的一种胆固醇依赖性溶细胞素,与单核细胞增生李斯特菌(Listeria monocytogenes)产生的溶血素O(LLO)在氨基酸序列上有80%的同源性。除了细胞溶解活性之外,LLO还显示出具有精氨酸诱导活性。为了确定LSO是否也能够表现出这两种不同的活性,我们构建了重组全长LSO(rLSO 530)和C端缺失的非细胞溶解性截短衍生物(rLSO 483),并将这些分子与重组LLO进行比较。当用胆固醇处理阻断细胞溶解活性时,细胞溶解rLSO 530分子可以诱导脾细胞中γ干扰素(IFN-γ)的产生。非细胞溶解性截短的rLSO 483分子也诱导IFN-γ产生。抗LLO多克隆抗体不仅抑制LLO诱导的IFN-γ产生,而且抑制LSO诱导的IFN-γ产生。NK细胞和CD 11b(+)细胞都是LSO诱导IFN-γ产生所必需的。在CD 11b(+)细胞表达的各种细胞因子中,白细胞介素-12(IL-12)和IL-18似乎是必需的。我们得出结论,LSO表现出与LLO相同的生物活性。
Seeligeriolysin O (LSO), one of the cholesterol-dependent cytolysins produced by Listeria seeligeri, shows 80% homology to listeriolysin O (LLO) produced by Listeria monocytogenes at the amino acid sequence level. In addition to cytolytic activity, LLO has been shown to exhibit cytokine-inducing activity. In order to determine whether LSO is also capable of exhibiting these two different activities, we constructed a recombinant full-length LSO (rLSO530) and a noncytolytic truncated derivative with a C-terminal deletion (rLSO483) and compared these molecules with recombinant LLO. The cytolytic rLSO530 molecule could induce gamma interferon (IFN-gamma) production in spleen cells when the cytolytic activity was blocked by treatment with cholesterol. The noncytolytic truncated rLSO483 molecule also induced IFN-gamma production. Anti-LLO polyclonal antibody inhibited not only LLO-induced IFN-gamma production but also LSO-induced IFN-gamma production. Both NK cells and CD11b(+) cells were required for LSO-induced IFN-gamma production. Among the various cytokines expressed in CD11b(+) cells, interleukin-12 (IL-12) and IL-18 appeared to be essential. We concluded that LSO exhibits the same biological activity as LLO.