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J. Biol. Chem., Vol. 279, Issue 37, 38693-38700, September 10, 2004

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Novel Protein-Protein Interactions of the Yersinia pestis Type III Secretion System Elucidated with a Matrix Analysis by Surface Plasmon Resonance and Mass Spectrometry^*

Wieslaw Swietnicki, Sarah O'Brien, Kari Holman, Scott Cherry, Ernst Brueggemann, Joseph E. Tropea, Harry B. Hines, David S. Waugh, and Robert G. Ulrich¶

From the United States Army Medical Research Institute of Infectious Diseases and the Macromolecular Crystallography Laboratory, NCI, National Institutes of Health, Frederick, Maryland 21702

Binary complexes formed by components of the Yersinia pestis type III secretion system were investigated by surface plasmon resonance (SPR) and matrix-assisted laser desorption time-of-flight mass spectrometry. Pairwise interactions between 15 recombinant Yersinia outer proteins (Yops), regulators, and chaperones were first identified by SPR. Mass spectrometry confirmed over 80% of the protein-protein interactions suggested by SPR, and new binding partners were further characterized. The Yop secretion protein (Ysc) M2 of Yersinia enterocolitica and LcrQ of Y. pestis, formerly described as ligands only for the specific Yop chaperone (Syc) H, formed stable complexes with SycE. Additional previously unreported complexes of YscE with the translocation regulator protein TyeA and the thermal regulator protein YmoA and multiple potential protein contacts by YscE, YopK, YopH, and LcrH were also identified. Because only stably folded proteins were examined, the interactions we identified are likely to occur either before or after transfer through the injectosome to mammalian host cells and may have relevance to understanding disease processes initiated by the plague bacterium.

Received for publication, May 11, 2004

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence and reprint requests should be addressed: Laboratory of Molecular Immunology, Army Medical Research Inst. of Infectious Diseases, 1425 Porter St., Frederick, MD 21702. E-mail: ulrich{at}ncifcrf.gov.

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