Lin Ching-Yi, Huang Yu-Shan, Li Chi-Han, Hsieh Yuan-Ting, Tsai Nu-Man, He Pei-Juin, Hsu Wei-Tung, Yeh Yi-Chen, Chiang Fang-Hsing, Wu Ming-Shiang, Chang Chia-Ching, Liao Kuang-Wen
Department of Biological Science and Technology, National Chiao-Tung University, Hsin-Chu, Taiwan.
Biochem Biophys Res Commun. 2009 Oct 16;388(2):283-9. doi: 10.1016/j.bbrc.2009.07.159. Epub 2009 Aug 5.
Helicobacter pylori heat shock protein 60 (HpHsp60) was first identified as an adhesion molecule associated with H. pylori infection. Here we have analyzed the structure of HpHsp60 via amino acid BLAST, circular dichroism, and electrophoresis and the results indicate that most recombinant HpHsp60 molecules exist as dimers or tetramers, which is quite different from Escherichia coli Hsp60. Treatment of human monocytic cells THP-1 with HpHsp60 was found to up-regulate a panel of cytokines including IL-1alpha, IL-8, IL-10, IFN-gamma, TNF-alpha, TGF-beta, GRO, and RANTES. Carboxymethylated HpHsp60 molecules with a switched oligomeric status were able to further enhance NF-kappaB-mediated IL-8 and TNF-alpha secretion in THP-1 cells compared to unmodified HpHsp60 molecules. These results indicated that the oligomeric status of HpHsp60s might have an important role in regulating host inflammation and thus help facilitate H. pylori persistent infection.
幽门螺杆菌热休克蛋白60（HpHsp60）最初被鉴定为与幽门螺杆菌感染相关的粘附分子。在此，我们通过氨基酸BLAST、圆二色性和电泳分析了HpHsp60的结构，结果表明大多数重组HpHsp60分子以二聚体或四聚体形式存在，这与大肠杆菌Hsp60有很大不同。发现用HpHsp60处理人单核细胞THP-1可上调一组细胞因子，包括IL-1α、IL-8、IL-10、IFN-γ、TNF-α、TGF-β、GRO和RANTES。与未修饰的HpHsp60分子相比，具有改变的寡聚状态的羧甲基化HpHsp60分子能够进一步增强THP-1细胞中NF-κB介导的IL-8和TNF-α分泌。这些结果表明，HpHsp60的寡聚状态可能在调节宿主炎症中起重要作用，从而有助于促进幽门螺杆菌的持续感染。
