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Infection and Immunity, November 2006, p. 6196-6205, Vol. 74, No. 11
0019-9567/06/$08.00+0     doi:10.1128/IAI.00753-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Amino Acid Residues within Enterohemorrhagic Escherichia coli O157:H7 Tir Involved in Phosphorylation, {alpha}-Actinin Recruitment, and Nck-Independent Pedestal Formation{triangledown}

Emma Allen-Vercoe, Barbara Waddell, Michael C. W. Toh, and Rebekah DeVinney*

Department of Microbiology and Infectious Diseases, University of Calgary Health Sciences Centre, 3330 Hospital Dr. NW, Calgary, Alberta T2N 4N1, Canada

Received 11 May 2006/ Returned for modification 28 June 2006/ Accepted 22 August 2006

Enterohemorrhagic Escherichia coli (EHEC) O157:H7 and enteropathogenic E. coli (EPEC) adherence to epithelial cells results in the formation of actin pedestals. Pedestal formation requires the bacterial protein Tir, which is inserted into the epithelial cell plasma membrane by the type III secretion system. EPEC and EHEC use different Tir-based mechanisms for pedestal formation, and the EPEC Tir residues required have been well described. In contrast, little is known about the regions of EHEC O157:H7 Tir that are essential for pedestal formation. Additionally, EHEC O157:H7 Tir is serine/threonine phosphorylated, although the residues involved and their role in pedestal formation are not known. In this study, we describe two regions within the carboxy terminus of EHEC O157:H7 Tir that are required for phosphorylation and pedestal formation. Serines 436 and 437 are substrates for protein kinase A phosphorylation, although this is not required to form pedestals. Using a series of internal deletion mutants, we found that amino acids 454 to 463 are required for efficient pedestal formation. Deleting this region resulted in a significant decrease in the recruitment of both filamentous actin and the actin binding protein {alpha}-actinin. As {alpha}-actinin binds directly to the EHEC O157:H7 amino terminus, these data suggest that its recruitment is dependent on pedestal formation.

* Corresponding author. Mailing address: Department of Microbiology and Infectious Diseases, University of Calgary Health Sciences Centre, 3330 Hospital Dr. NW, Calgary, AB T2N 4N1, Canada. Phone: (403) 220-4095. Fax: (403) 270-2772. E-mail: rdevinne{at}ucalgary.ca.

{triangledown} Published ahead of print on 5 September 2006.

Editor: F. C. Fang

Infection and Immunity, November 2006, p. 6196-6205, Vol. 74, No. 11
0019-9567/06/$08.00+0     doi:10.1128/IAI.00753-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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