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Identification of two protein-binding and functional regions of curli, a surface organelle and virulence determinant of Escherichia coli

Olsén, Arne LU ; Herwald, Heiko LU ; Wikstrom, M; Persson, Kristin LU ; Mattsson, Eva LU and Björck, Lars LU (2002) In Journal of Biological Chemistry 277(37). p.34568-34572
Abstract
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.... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
277
issue
37
pages
34568 - 34572
publisher
ASBMB
external identifiers
  • wos:000177959100130
  • scopus:0037072888
ISSN
1083-351X
DOI
10.1074/jbc.M206353200
language
English
LU publication?
yes
id
60eb2c75-a128-4fab-9889-46f31fd0a0e1 (old id 328576)
date added to LUP
2007-11-02 14:18:02
date last changed
2017-12-17 03:32:47
@article{60eb2c75-a128-4fab-9889-46f31fd0a0e1,
  abstract     = {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.},
  author       = {Olsén, Arne and Herwald, Heiko and Wikstrom, M and Persson, Kristin and Mattsson, Eva and Björck, Lars},
  issn         = {1083-351X},
  language     = {eng},
  number       = {37},
  pages        = {34568--34572},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Identification of two protein-binding and functional regions of curli, a surface organelle and virulence determinant of Escherichia coli},
  url          = {http://dx.doi.org/10.1074/jbc.M206353200},
  volume       = {277},
  year         = {2002},
}