Bordetella dermonecrotic toxin binds to target cells via the N-terminal 30 amino acids
Bordetella dermonecrotic toxin binds to target cells via the N-terminal 30 amino acids
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DOI：
10.1111/j.1348-0421.2010.00300.x
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发表时间：
2011-03-01
影响因子：
2.6
通讯作者：
Horiguchi, Yasuhiko
中科院分区：
文献类型：
--
作者：
Fukui-Miyazaki, Aya;Ohnishi, Shinya;Horiguchi, Yasuhiko
德氏波氏杆菌毒素(DNT)通过激活细胞内Rho GTP酶而影响宿主细胞的生物学功能。该毒素通过54个N端氨基酸与未知受体(S)结合，在Arg44的C端被呋喃或呋喃类蛋白酶分子内切割，最终进入Rho GTP酶所在的细胞质。DNT与受体(S)的结合和分子内切割是DNT中毒细胞所必需的，54个氨基酸结合区包围着切割部位，但这两个事件是否相关尚不清楚。在这项研究中，我们可以将细胞结合区域缩小到N端氨基酸2-30。该区域不包含Furin识别位点，表明细胞结合和分子内切割是独立的事件。
Bordetella dermonecrotic toxin (DNT) affects the biological function of host cells by activating intracellular Rho GTPases. The toxin binds to unidentified receptor(s) via 54 N-terminal amino acids, undergoes intramolecular cleavage on the C-terminal side of Arg44 by furin or furin-like protease, and eventually enters the cytoplasm where the Rho GTPases reside. The binding to the receptor(s) and intramolecular cleavage are essential for DNT to intoxicate cells, and the 54 amino-acid binding domain encompasses the cleavage site, however, it is unclear whether these two events are related. In this study, we could narrow down the cell-binding domain to the N-terminal amino acids 2-30. The region does not contain the furin-recognition site, indicating that the cell binding and the intramolecular cleavage are independent events.