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Bordetella pertussis binds to human C4b-binding protein (C4BP) at a site similar to that used by the natural ligand C4b

Berggård, Karin LU ; Lindahl, Gunnar LU ; Dahlbäck, Björn LU and Blom, Anna LU (2001) In European Journal of Immunology 31(9). p.2771-2780
Abstract
Human complement regulators are important targets for pathogenic microorganisms. In one such interaction, Bordetella pertussis binds human C4b-binding protein (C4BP), a high-molecular-weight plasma protein that acts as inhibitor of the classical pathway of complement activation. At least two different B. pertussis surface components, one of which is the virulence factor filamentous hemagglutinin (FHA), contribute to the binding. We used a set of C4BP mutants and monoclonal antibodies to characterize the region in C4BP that binds B. pertussis and analyzed the salt sensitivity of the interaction. These studies indicated that positively charged residues at the interface between complement control protein modules 1-2 in the C4BP alpha-chain... (More)
Human complement regulators are important targets for pathogenic microorganisms. In one such interaction, Bordetella pertussis binds human C4b-binding protein (C4BP), a high-molecular-weight plasma protein that acts as inhibitor of the classical pathway of complement activation. At least two different B. pertussis surface components, one of which is the virulence factor filamentous hemagglutinin (FHA), contribute to the binding. We used a set of C4BP mutants and monoclonal antibodies to characterize the region in C4BP that binds B. pertussis and analyzed the salt sensitivity of the interaction. These studies indicated that positively charged residues at the interface between complement control protein modules 1-2 in the C4BP alpha-chain are important for binding, and that the site in C4BP that binds B. pertussis is very similar, but not identical, to the C4b-binding site. Bacteria-bound C4BP retained its complement regulatory function and B. pertussis selectively bound C4BP in human plasma, indicating that binding occurs also in vivo. Together, these findings indicate that B. pertussis exploits a site in C4BP, resembling that used by the natural ligand C4b. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
European Journal of Immunology
volume
31
issue
9
pages
2771 - 2780
publisher
John Wiley & Sons
external identifiers
  • pmid:11536176
  • scopus:0034801718
ISSN
1521-4141
DOI
10.1002/1521-4141(200109)31:9<2771::AID-IMMU2771>3.0.CO;2-0
language
English
LU publication?
yes
id
8d88b016-d608-4727-8453-a5cab72e68dd (old id 1120516)
date added to LUP
2008-06-24 14:15:43
date last changed
2018-01-07 06:10:28
@article{8d88b016-d608-4727-8453-a5cab72e68dd,
  abstract     = {Human complement regulators are important targets for pathogenic microorganisms. In one such interaction, Bordetella pertussis binds human C4b-binding protein (C4BP), a high-molecular-weight plasma protein that acts as inhibitor of the classical pathway of complement activation. At least two different B. pertussis surface components, one of which is the virulence factor filamentous hemagglutinin (FHA), contribute to the binding. We used a set of C4BP mutants and monoclonal antibodies to characterize the region in C4BP that binds B. pertussis and analyzed the salt sensitivity of the interaction. These studies indicated that positively charged residues at the interface between complement control protein modules 1-2 in the C4BP alpha-chain are important for binding, and that the site in C4BP that binds B. pertussis is very similar, but not identical, to the C4b-binding site. Bacteria-bound C4BP retained its complement regulatory function and B. pertussis selectively bound C4BP in human plasma, indicating that binding occurs also in vivo. Together, these findings indicate that B. pertussis exploits a site in C4BP, resembling that used by the natural ligand C4b.},
  author       = {Berggård, Karin and Lindahl, Gunnar and Dahlbäck, Björn and Blom, Anna},
  issn         = {1521-4141},
  language     = {eng},
  number       = {9},
  pages        = {2771--2780},
  publisher    = {John Wiley & Sons},
  series       = {European Journal of Immunology},
  title        = {Bordetella pertussis binds to human C4b-binding protein (C4BP) at a site similar to that used by the natural ligand C4b},
  url          = {http://dx.doi.org/10.1002/1521-4141(200109)31:9<2771::AID-IMMU2771>3.0.CO;2-0},
  volume       = {31},
  year         = {2001},
}