Zhang Jing, Zhang Yu, Li Zhiqiang, Liu Jing, Shao Xuehua, Wu Changxin, Wang Yong, Wang Kaisheng, Li Tiansen, Liu Laizhen, Chen Chuangfu, Zhang Hui
College of Animal Science and Technology, Shihezi University, Shihezi, China.
School of Biotechnology and Food, Shangqiu Normal University, Shangqiu, China.
Front Vet Sci. 2017 Dec 13;4:197. doi: 10.3389/fvets.2017.00197. eCollection 2017.
Outer membrane protein 25 (OMP25), a virulence factor from , plays an important role in maintaining the structural stability of . Mitogen-activated protein kinase (MAPK) signal pathway widely exists in eukaryotic cells. In this study, human trophoblast cell line HPT-8 and BALB/c mice were infected with 2308 strain (S2308) and 2308ΔOmp25 mutant strain. The expression of cytokines and activation of MAPK signal pathway were detected. We found that the expressions of tumor necrosis factor-α, interleukin-1, and interleukin-10 (IL-10) were increased in HPT-8 cells infected with S2308 and 2308ΔOmp25 mutant. S2308 also activated p38 phosphorylation protein, extracellular-regulated protein kinases (ERK), and Jun-N-terminal kinase (JNK) from MAPK signal pathway. 2308ΔOmp25 could not activate p38, ERK, and JNK branches. Immunohistochemistry experiments showed that S2308 was able to activate phosphorylation of p38 and ERK in BABL/c mice. However, 2308ΔOmp25 could weakly activate phosphorylation of p38 and ERK. These results suggest that Omp25 played an important role in the process of activation of the MAPK signal pathway.
外膜蛋白25（OMP25）是[病原体名称]的一种毒力因子，在维持[病原体名称]的结构稳定性方面发挥着重要作用。丝裂原活化蛋白激酶（MAPK）信号通路广泛存在于真核细胞中。在本研究中，人滋养层细胞系HPT-8和BALB/c小鼠分别感染了[病原体名称]2308菌株（S2308）和2308ΔOmp25突变株。检测了细胞因子的表达和MAPK信号通路的激活情况。我们发现，感染S2308和2308ΔOmp25突变株的HPT-8细胞中肿瘤坏死因子-α、白细胞介素-1和白细胞介素-10（IL-10）的表达均增加。S2308还激活了MAPK信号通路中的p38磷酸化蛋白、细胞外调节蛋白激酶（ERK）和Jun氨基末端激酶（JNK）。2308ΔOmp25不能激活p38、ERK和JNK分支。免疫组织化学实验表明，S2308能够激活BABL/c小鼠中p38和ERK的磷酸化。然而，2308ΔOmp25只能微弱地激活p38和ERK的磷酸化。这些结果表明，Omp25在MAPK信号通路的激活过程中发挥了重要作用。
