Differential recognition of members of the carcinoembryonic antigen family by Afa/Dr adhesins of diffusely adhering Escherichia coli (Afa/Dr DAEC).
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.
Berger
Cedric N
CN
Institut National de la Santé et de la Recherche Médicale (INSERM), Unité 510, Faculté de Pharmacie Paris XI, F-92296 Châtenay-Malabry, France.
Billker
Oliver
O
Meyer
Thomas F
TF
Servin
Alain L
AL
Kansau
Imad
I
D018830:Adhesins, Escherichia coli / Q000378:metabolism*; D000818:Animals; D000942:Antigens, Bacterial / Q000378:metabolism*; D015703:Antigens, CD / Q000378:metabolism; D000943:Antigens, Differentiation / Q000378:metabolism; D000951:Antigens, Neoplasm / Q000378:metabolism; D001422:Bacterial Adhesion; D018958:CD55 Antigens / Q000378:metabolism; D016466:CHO Cells; D002272:Carcinoembryonic Antigen / Q000378:metabolism*; D015815:Cell Adhesion Molecules / Q000378:metabolism; D002460:Cell Line; D006224:Cricetinae; D004268:DNA-Binding Proteins / Q000378:metabolism; D004926:Escherichia coli / Q000472:pathogenicity*; D029968:Escherichia coli Proteins / Q000378:metabolism*; D036781:Fimbriae Proteins / Q000378:metabolism*; D058851:GPI-Linked Proteins; D006367:HeLa Cells; D006388:Hemagglutinins / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D014157:Transcription Factors / Q000378:metabolism; D020764:cdc42 GTP-Binding Protein / Q000378:metabolism
D018830:Adhesins, Escherichia coli; C108509:AfaE protein, E coli; D000942:Antigens, Bacterial; D015703:Antigens, CD; D000943:Antigens, Differentiation; D000951:Antigens, Neoplasm; D018958:CD55 Antigens; C069847:CD66 antigens; C075729:CEACAM3 protein, human; C504117:CEACAM6 protein, human; D002272:Carcinoembryonic Antigen; D015815:Cell Adhesion Molecules; D004268:DNA-Binding Proteins; C465564:Dr adhesin, E coli; C086680:ETV5 protein, human; D029968:Escherichia coli Proteins; D058851:GPI-Linked Proteins; D006388:Hemagglutinins; D014157:Transcription Factors; C080952:DaaE protein, E coli; D036781:Fimbriae Proteins; D020764:cdc42 GTP-Binding Protein