Heat-labile enterotoxin: beyond G(m1) binding.
Heat-labile enterotoxin: beyond G(m1) binding.
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DOI：
10.3390/toxins2061445
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发表时间：
2010-06
期刊：
影响因子：
4.2
通讯作者：
Kuehn MJ
中科院分区：
文献类型：
--
作者：
Mudrak B;Kuehn MJ
产肠毒素大肠杆菌（ETEC）是世界范围内发病率和死亡率的重要来源。ETEC释放的一个主要毒力因子是不耐热肠毒素LT，其结构和功能与霍乱毒素相似。LT由五个B亚基携带一个催化活性的A亚基组成。LTB与毒素的宿主受体单唾液酸神经节苷脂GM1结合，但与A型血糖和E.大肠杆菌脂多糖也在过去十年中被鉴定。在这里，我们回顾了LT B亚基五聚体的调节、组装和结合特性，并讨论了其众多分子相互作用的可能作用。
Enterotoxigenic Escherichia coli (ETEC) is a significant source of morbidity and mortality worldwide. One major virulence factor released by ETEC is the heat-labile enterotoxin LT, which is structurally and functionally similar to cholera toxin. LT consists of five B subunits carrying a single catalytically active A subunit. LTB binds the monosialoganglioside GM1, the toxin’s host receptor, but interactions with A-type blood sugars and E. coli lipopolysaccharide have also been identified within the past decade. Here, we review the regulation, assembly, and binding properties of the LT B-subunit pentamer and discuss the possible roles of its numerous molecular interactions.