Sokolova Olga, Heppel Nicole, Jägerhuber Ruth, Kim Kwang Sik, Frosch Matthias, Eigenthaler Martin, Schubert-Unkmeir Alexandra
Institute of Hygiene and Microbiology, University of Wuerzburg, Germany.
Cell Microbiol. 2004 Dec;6(12):1153-66. doi: 10.1111/j.1462-5822.2004.00422.x.
Neisseria meningitidis traversal across the blood-cerebrospinal fluid barrier is an essential step in the pathogenesis of bacterial meningitis. We have previously shown that invasion of human brain microvascular endothelial cells (HBMEC) by meningococci is mediated by bacterial outer membrane protein Opc that binds fibronectin, thereby anchoring the bacterium to the integrin alpha 5 beta 1-receptor on the endothelial cell surface. However, subsequent signal transduction mechanisms essential for or regulated by N. meningitidis adhesion and invasion, or HBMEC responses to N. meningitidis are unknown. In this report we investigated the role of c-Jun N-terminal kinases 1 and 2 (JNK1 and JNK2), p38 mitogen-activated (MAP) kinase and protein tyrosine kinases in endothelial-N. meningitidis interaction. Binding of meningococci to HBMEC phosphorylated and activated JNK1 and JNK2 and p38 MAPK as well as their direct substrates c-Jun and MAP kinase activated kinase-2 (MAPKAPK-2), respectively. Non-invasive meningococcal strains lacking opc gene (opc mutants and sequence type 11 complex meningococci) still activated p38 MAPK, however, failed to activate JNK. Inhibition of JNK1 and JNK2 significantly reduced internalization of N. meningitidis by HBMEC without affecting its adherence. Blocking the endothelial integrin alpha 5 beta 1 also decreased N. meningitidis-induced JNK activation in HBMEC. These findings indicate the crucial role of JNK signalling pathway in N. meningitidis invasion in HBMEC. In contrast, p38 MAPK pathway was important for the control of interleukin-6 (IL-6) and IL-8 release by HBMEC. Genistein, a protein tyrosine kinase inhibitor, decreased both invasion of N. meningitidis into HBMEC and IL-6 and IL-8 release, indicating that protein tyrosine kinases, which link signals from integrins to intracellular signalling pathways are essential for both bacterial internalization and cytokine secretion by HBMEC.
脑膜炎奈瑟菌穿越血脑屏障是细菌性脑膜炎发病机制中的关键步骤。我们之前已表明,脑膜炎球菌对人脑血管内皮细胞(HBMEC)的侵袭由结合纤连蛋白的细菌外膜蛋白Opc介导,从而将细菌锚定在内皮细胞表面的整合素α5β1受体上。然而,脑膜炎奈瑟菌黏附与侵袭所必需的或受其调控的后续信号转导机制,或HBMEC对脑膜炎奈瑟菌的反应尚不清楚。在本报告中,我们研究了c-Jun氨基末端激酶1和2(JNK1和JNK2)、p38丝裂原活化(MAP)激酶和蛋白酪氨酸激酶在内皮细胞与脑膜炎奈瑟菌相互作用中的作用。脑膜炎球菌与HBMEC的结合分别使JNK1和JNK2以及p38 MAPK及其直接底物c-Jun和丝裂原活化蛋白激酶激活的激酶-2(MAPKAPK-2)磷酸化并激活。缺乏opc基因的非侵袭性脑膜炎球菌菌株(opc突变体和序列型11复合体脑膜炎球菌)仍能激活p38 MAPK,但无法激活JNK。抑制JNK1和JNK2可显著降低HBMEC对脑膜炎奈瑟菌的内化,而不影响其黏附。阻断内皮整合素α5β1也会降低HBMEC中脑膜炎奈瑟菌诱导的JNK激活。这些发现表明JNK信号通路在脑膜炎奈瑟菌侵袭HBMEC中起关键作用。相比之下,p38 MAPK通路对控制HBMEC释放白细胞介素-6(IL-6)和IL-8很重要。蛋白酪氨酸激酶抑制剂染料木黄酮可降低脑膜炎奈瑟菌对HBMEC的侵袭以及IL-6和IL-8的释放,这表明将整合素信号与细胞内信号通路联系起来的蛋白酪氨酸激酶对HBMEC的细菌内化和细胞因子分泌都至关重要。