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Infection and Immunity, March 2001, p. 1444-1453, Vol. 69, No. 3
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.3.1444-1453.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Enteropathogenic Escherichia coli (EPEC) Tir Receptor Molecule Does Not Undergo Full Modification When Introduced into Host Cells by EPEC-Independent Mechanisms

Brendan Kenny* and Jonathan Warawa

Department of Pathology and Microbiology, School of Medical Sciences, University Walk, Bristol BS8 1TD, England

Received 7 August 2000/Returned for modification 30 October 2000/Accepted 7 December 2000

Enteropathogenic Escherichia coli (EPEC), like many other gram-negative pathogens, encodes a type III secretion apparatus dedicated to the release of virulence-associated proteins. One such protein, Tir, is translocated into host cells, where it is modified by the addition of phosphate groups, resulting in a number of species with distinct molecular mass. One phosphorylation event, on tyrosine residue 474 of Tir, does not contribute to shifts in molecular mass but is essential for its actin-nucleating function. The role of the nonphosphotyrosine related modifications is unknown. In this paper, we demonstrate, using three different approaches, that Tir does not encode sufficient information to facilitate its complete modification when introduced into host cells in EPEC-independent mechanisms. Each system revealed that Tir is a substrate for a host kinase whose action results in its partial modification to a form similar to one evident in EPEC-infected host cells. Further Tir modification could not be induced by infecting cells with EPEC, suggesting that Tir must be coexpressed with other EPEC factors to enable its full modification within host cells. One approach used Yersinia spp. to deliver Tir into host cells, and this system revealed that Tir secretion and translocation can occur in the absence of the Tir chaperone molecule, CesT (formerly known as OrfU). CesT was found to be an efficiency factor which was not required, unlike in EPEC, for Tir stability, indicating that it may function to guide Tir to the translocation apparatus or maintain it in a secretion-competent form.

* Corresponding author. Mailing address: Department of Pathology and Microbiology, School of Medical Sciences, University Walk, Bristol BS8 1TD, England. Phone: (0117) 928 7530. Fax: (0117) 930 0543. E-mail: B.Kenny{at}bristol.ac.uk.

Infection and Immunity, March 2001, p. 1444-1453, Vol. 69, No. 3
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.3.1444-1453.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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