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Originally published In Press as doi:10.1074/jbc.M206353200 on July 3, 2002

J. Biol. Chem., Vol. 277, Issue 37, 34568-34572, September 13, 2002
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Identification of Two Protein-binding and Functional Regions of Curli, a Surface Organelle and Virulence Determinant of Escherichia coli*

Arne OlsénDagger §, Heiko HerwaldDagger , Mats Wikström, Kristin PerssonDagger , Eva MattssonDagger ||, and Lars BjörckDagger

From the Dagger  Section for Molecular Pathogenesis, Department of Cell and Molecular Biology, Lund University, SE-221 84 Lund, Sweden,  Biovitrum, SE-112 87 Stockholm, Sweden, and the || Department of Medical Microbiology, Dermatology, and Infection, Lund University Hospital, SE-221 85 Lund, Sweden

Curli are surface organelles of Escherichia coli. These fibrous proteins, formed by polymerization of a 15-kDa subunit, are expressed by E. coli strains associated with severe infections in humans. A remarkable property of curli is their ability to interact with a wide range of human proteins, interactions that contribute to the enhanced virulence of curli-expressing E. coli. To define the protein-binding region(s) of curli, we investigated the binding properties of overlapping synthetic peptides covering the curli subunit. Two peptides, one covering a 24-amino acid residue sequence in the NH2-terminal half of the subunit (NNS24) and one corresponding to the 26 COOH-terminal residues (VDQ26), were found to bind a number of human proteins. Physiochemical analysis revealed that NNS24 adopts a thermally stable beta -structure, and in solution the peptide forms soluble multimers, predominantly octamers. Intact curli are known to activate the proinflammatory and procoagulant contact system, and when added to human plasma, the NNS24 and VDQ26 peptides induced the release of the potent vasoactive peptide bradykinin. The results map important curli functions to the regions corresponding to the NNS24 and VDQ26 sequences.

* This work was supported by grants from the Swedish Research Council (Projects 7480, 13413, and 14272), the Crafoord, Bergvall, Kock, Nilson, and Österlund Foundations, the Royal Physiografic Society in Lund, the Medical Faculty, Lund University, and Hansa Medical AB.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed: Dept. of Clinical Immunology, Göteborg University, Guldhedsgatan 10A, SE-413 46 Göteborg, Sweden. Tel.: 46-31-342-4895; Fax: 46-31-342-4621; E-mail: arne.olsen@immuno.gu.se.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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