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Infection and Immunity, May 2006, p. 2676-2685, Vol. 74, No. 5
0019-9567/06/$08.00+0     doi:10.1128/IAI.74.5.2676-2685.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Outer Membrane Protein A of Escherichia coli O157:H7 Stimulates Dendritic Cell Activation

Alfredo G. Torres,^1,2,3,* Yongguo Li,^1,, Christopher B. Tutt,¹ Lijun Xin,¹ Tonyia Eaves-Pyles,¹ and Lynn Soong^1,2,3*

Departments of Microbiology and Immunology,¹ Pathology,² Sealy Center for Vaccine Development, University of Texas Medical Branch, Galveston, Texas 77555-1070³

Received 21 September 2005/ Returned for modification 22 November 2005/ Accepted 15 February 2006

Outer membrane protein A (OmpA) is located in the membrane of Escherichia coli and other gram-negative bacteria and plays a multifunctional role in bacterial physiology and pathogenesis. In enterohemorrhagic E. coli (EHEC), especially serotype O157:H7, OmpA interacts with cultured human intestinal cells and likely acts as an important component to stimulate the immune response during infection. To test this hypothesis, we analyzed the effect of EHEC OmpA on cytokine production by dendritic cells (DCs) and on DC migration across polarized intestinal epithelial cells. OmpA induced murine DCs to secrete interleukin-1 (IL-1), IL-10, and IL-12 in a dose-dependent manner, and this effect was independent of Toll-like receptor 4. Although DCs displayed differential responses to EHEC OmpA and OmpA-specific antibodies enhanced DC cytokine secretion, we cannot discard that other EHEC surface elements were likely to be involved. While OmpA was required for bacterial binding to polarized Caco-2 cells, it was not needed for the induction of cytokine production by Caco-2 cells or for human DC migration across polarized cells.

Editor: A. D. O'Brien

Present address: Department of Infectious Diseases, The First Clinical Medical College of Harbin Medical University, Heilongjiang Province 150001, People's Republic of China.

A.G.T. and Y.L. contributed equally to this work.

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