Mycoplasma pneumoniae CARDS toxin is internalized via clathrin-mediated endocytosis.
Mycoplasma pneumoniae CARDS toxin is internalized via clathrin-mediated endocytosis.
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DOI：
10.1371/journal.pone.0062706
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发表时间：
2013
期刊：
影响因子：
3.7
通讯作者：
Baseman JB
中科院分区：
文献类型：
--
作者：
Krishnan M;Kannan TR;Baseman JB
细菌毒素具有特定的结合和摄取哺乳动物细胞的机制。肺炎支原体CADS(社区获得性呼吸窘迫综合征)毒素是一种68 kDa的蛋白，与人表面活性蛋白A具有高亲和力，并具有单腺苷二磷酸核糖化和空泡化等独特的生物活性。这些特性导致呼吸道的炎症过程和一系列的细胞病理学，包括纤毛停滞、组织完整性和损伤的丧失以及细胞死亡。然而，CARDS毒素进入靶细胞的过程尚不清楚。在这项研究中，我们发现CARDS毒素结合到哺乳动物细胞表面，并通过网状蛋白介导的途径以剂量和时间依赖的方式迅速内化，这表明毒素内化被单丹西林抑制，但不被甲基-β-环糊精或菲利平所抑制。此外，在网状蛋白耗竭的细胞中，CADS毒素的内化明显受到抑制。
Bacterial toxins possess specific mechanisms of binding and uptake by mammalian cells. Mycoplasma pneumoniae CARDS (Community Acquired Respiratory Distress Syndrome) toxin is a 68 kDa protein, which demonstrates high binding affinity to human surfactant protein-A and exhibits specific biological activities including mono-ADP ribosylation and vacuolization. These properties lead to inflammatory processes in the airway and a range of cytopathologies including ciliostasis, loss of tissue integrity and injury, and cell death. However, the process by which CARDS toxin enters target cells is unknown. In this study, we show that CARDS toxin binds to mammalian cell surfaces and is internalized rapidly in a dose and time-dependent manner using a clathrin-mediated pathway, as indicated by inhibition of toxin internalization by monodansylcadaverine but not by methyl-β-cyclodextrin or filipin. Furthermore, the internalization of CARDS toxin was markedly inhibited in clathrin-depleted cells.
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影响因子：
3.7
作者：
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通讯作者：
Baseman JB
影响因子：
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