Differential recognition of members of the carcinoembryonic antigen family by Afa/Dr adhesins of diffusely adhering Escherichia coli (Afa/Dr DAEC)
Differential recognition of members of the carcinoembryonic antigen family by Afa/Dr adhesins of diffusely adhering Escherichia coli (Afa/Dr DAEC)
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DOI：
10.1111/j.1365-2958.2004.04033.x
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发表时间：
2004-05-01
影响因子：
3.6
通讯作者：
Kansau, I
中科院分区：
文献类型：
--
作者：
Berger, CN;Billker, O;Kansau, I
关于弥漫性粘附大肠杆菌（DAEC）携带Afa/Dr粘附素家族的毒力的分子基础知之甚少。这些粘附素识别GPI锚定蛋白CD 55（衰变加速因子，CD 55）和CD 66 e（癌胚抗原，CEA）作为受体。CD 66 e是CEA相关细胞粘附分子（CEACAM）家族的成员，包括七个成员。我们使用表达CEACAM的CHO和HeLa细胞分析了Afa/Dr DAEC与CEACAM的相互作用。结果表明，只有E.表达Afa/Dr粘附素亚家族的大肠杆菌，在此命名为Afa/Dr-I，包括Dr、F1845和AfaE-III粘附素，结合到表达CEACAM 1、CEA或CEACAM 6的CHO细胞上。尽管所有的Afa/Dr粘附素都引起粘附细菌周围的CD 55的募集，但只有Afa/Dr-I亚家族引起CEACAM 1、CEA和CEACAM 6的募集。此外，尽管CEACAM 3不被Afa/Dr粘附素亚家族识别为受体，但它在HeLa细胞中被招募到细菌周围。粘附细菌周围募集的CEACAM 1、CEA和CEACAM 6完全或部分抵抗去污剂提取，而募集的CEACAM 3不抵抗。最后，结果表明，CEA和CEACAM 6而不是CEACAM 1的识别伴随着细胞表面微绒毛样延伸物与细菌的紧密附着，所述微绒毛样延伸物是细长的。此外，CEA的识别伴随着Rho GT3 Cdc 42的激活和ERM的磷酸化，这反过来又引起观察到的细胞表面微绒毛样延伸。
Little is known about the molecular bases underlying the virulence of diffusely adhering Escherichia coli (DAEC) harbouring the Afa/Dr family of adhesins. These adhesins recognize as receptors the GPI-anchored proteins CD55 (decay-accelerating factor, DAF) and CD66e (carcinoembryonic antigen, CEA). CD66e is a member of the CEA-related cell adhesion molecules (CEACAM) family, comprising seven members. We analysed the interactions of Afa/Dr DAEC with the CEACAMs using CEACAM-expressing CHO and HeLa cells. The results demonstrate that only E. coli expressing a subfamily of Afa/Dr adhesins, named here Afa/Dr-I, including Dr, F1845 and AfaE-III adhesins, bound onto CHO cells expressing CEACAM1, CEA or CEACAM6. Whereas all the Afa/Dr adhesins elicit recruitment of CD55 around adhering bacteria, only the Afa/Dr-I subfamily elicits the recruitment of CEACAM1, CEA and CEACAM6. In addition, although CEACAM3 is not recognized as a receptor by the subfamily of Afa/Dr adhesins, it is recruited around bacteria in HeLa cells. The recruited CEACAM1, CEA and CEACAM6 around adhering bacteria resist totally or in part a detergent extraction, whereas the recruited CEACAM3 does not. Finally, the results show that recognition of CEA and CEACAM6, but not CEACAM1, is accompanied by tight attachment to bacteria of cell surface microvilli-like extensions, which are elongated. Moreover, recognition of CEA is accompanied by an activation of the Rho GTPase Cdc42 and by a phosphorylation of ERM, which in turn elicit the observed cell surface microvilli-like extensions.