| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 277, Issue 37, 34568-34572, September 13, 2002
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the 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
Identification of Two Protein-binding and Functional Regions
of Curli, a Surface Organelle and Virulence Determinant of
Escherichia coli*
§,,,
, and
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
-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.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  A. P. White, D. L. Gibson, G. A. Grassl, W. W. Kay, B. B. Finlay, B. A. Vallance, and M. G. Surette Aggregation via the Red, Dry, and Rough Morphotype Is Not a Virulence Adaptation in Salmonella enterica Serovar Typhimurium Infect. Immun., March 1, 2008; 76(3): 1048 - 1058. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. L. Gibson, A. P. White, C. M. Rajotte, and W. W. Kay AgfC and AgfE facilitate extracellular thin aggregative fimbriae synthesis in Salmonella Enteritidis Microbiology, April 1, 2007; 153(4): 1131 - 1140. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. J. Alteri, J. Xicohtencatl-Cortes, S. Hess, G. Caballero-Olin, J. A. Giron, and R. L. Friedman Mycobacterium tuberculosis produces pili during human infection PNAS, March 20, 2007; 104(12): 5145 - 5150. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 X. Wang, D. R. Smith, J. W. Jones, and M. R. Chapman In Vitro Polymerization of a Functional Escherichia coli Amyloid Protein J. Biol. Chem., February 9, 2007; 282(6): 3713 - 3719. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 W. Bokranz, X. Wang, H. Tschape, and U. Romling Expression of cellulose and curli fimbriae by Escherichia coli isolated from the gastrointestinal tract J. Med. Microbiol., December 1, 2005; 54(12): 1171 - 1182. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. P. White, D. L. Gibson, S. K. Collinson, P. A. Banser, and W. W. Kay Extracellular Polysaccharides Associated with Thin Aggregative Fimbriae of Salmonella enterica Serovar Enteritidis J. Bacteriol., September 15, 2003; 185(18): 5398 - 5407. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. Persson, W. Russell, M. Morgelin, and H. Herwald The Conversion of Fibrinogen to Fibrin at the Surface of Curliated Escherichia coli Bacteria Leads to the Generation of Proinflammatory Fibrinopeptides J. Biol. Chem., August 22, 2003; 278(34): 31884 - 31890. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
X. Zogaj, W. Bokranz, M. Nimtz, and U. Romling Production of Cellulose and Curli Fimbriae by Members of the Family Enterobacteriaceae Isolated from the Human Gastrointestinal Tract Infect. Immun., July 1, 2003; 71(7): 4151 - 4158. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
