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(American Journal of Pathology. 2004;164:763-772.)
© 2004 American Society for Investigative Pathology

Short Communication

Bacterial Chaperone Protein, Skp, Induces Leukocyte Chemotaxis via C5a Receptor

Arjun Shrestha*, Lei Shi{dagger}, Sumio Tanase{ddagger}, Makiko Tsukamoto§, Norikazu Nishino§, Kazutaka Tokita* and Tetsuro Yamamoto*

From the Departments of Molecular Pathology*and Medical Biochemistry,{ddagger}Faculty of Medical and Pharmaceutical Sciences, and the Department of Molecular Pathology,{dagger}Graduate School of Medical Sciences, Kumamoto University, Kumamoto; and the Department of Biological Functions and Engineering,§Graduate School of Life Science and Systems Engineering, Kyushu Institute of Technology, Kitakyushu, Japan

C5a receptor has been identified as a leukocyte chemotactic receptor to two intrinsic chemical mediators, C5a and the S19 ribosomal protein dimer, so far. We found an Escherichia coli protein that also induced the chemotactic responses of monocytes and polymorphonuclear leukocytes via the C5a receptor. We identified the E. coli-derived chemoattractant to be Skp by the molecular size and the N-terminal amino acid sequence. Skp is a periplasmic chaperone protein widely present in gram-negative bacterial species. Immunoabsorption experiments indicated that Skp was the major leukocyte chemotactic factor in the E. coli extract. Receptor-antagonizing experiments with analogue peptides of S19 ribosomal protein and of C5a suggested that Skp induced the receptor activation by the two-step binding mechanism as in the cases of the intrinsic mediators, sharing the ligand-binding site of the receptor among them at each binding step. The C5a receptor would play a role in the host defense directly recognizing the bacteria-derived protein, besides identifying the signals of the intrinsic chemical mediators.






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Copyright © 2004 by the American Society for Investigative Pathology.