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Localization of functional sites in the viral complement inhibitor KCP

Mark, Linda LU ; Spiller, OB; Villoutreix, BO and Blom, AM (2004) 12th Annual International Congress of Immunology/4th Annual Conference of the Federation-of-Clinical-Immunology-Societies (FOCIS) In Immunology 2004: Cytokine Network, Regulatory Cells, Signaling, and Apoptosis p.243-247
Abstract
Kaposi's sarcoma-associated herpes virus (KSHV) encodes a complement inhibitor named KSHV complement control protein (KCP). We have previously shown that KCP inhibits the human complement system by disrupting the C3 convertase of complement. KCP can accelerate the decay of the classical C3 convertase and it can act as a cofactor for factor I (R), which then cleaves and inactivates C4b or C3b (in the classical and alternative convertase, respectively). The aim of this study was to 1) delineate the sites on KCP responsible for complement inhibition 2) study the binding of KCP to heparin and the surface of cells. We constructed a 3D model of the four CCP domains KCP by homology based modeling, which served as basis for site directed... (More)
Kaposi's sarcoma-associated herpes virus (KSHV) encodes a complement inhibitor named KSHV complement control protein (KCP). We have previously shown that KCP inhibits the human complement system by disrupting the C3 convertase of complement. KCP can accelerate the decay of the classical C3 convertase and it can act as a cofactor for factor I (R), which then cleaves and inactivates C4b or C3b (in the classical and alternative convertase, respectively). The aim of this study was to 1) delineate the sites on KCP responsible for complement inhibition 2) study the binding of KCP to heparin and the surface of cells. We constructed a 3D model of the four CCP domains KCP by homology based modeling, which served as basis for site directed mutagenesis. A patch of positively charged amino acids in CCPI, stretching into CCP2 as well as a positive and a negative patch in the region between CCP2-3 were the most functionally important sites. KCP binds to heparin and the surface of cells via a site in CCPI. (Less)
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author
organization
publishing date
type
Chapter in Book/Report/Conference proceeding
publication status
published
subject
in
Immunology 2004: Cytokine Network, Regulatory Cells, Signaling, and Apoptosis
pages
243 - 247
publisher
Medimond
conference name
12th Annual International Congress of Immunology/4th Annual Conference of the Federation-of-Clinical-Immunology-Societies (FOCIS)
external identifiers
  • WOS:000227166900045
language
English
LU publication?
yes
id
dcac0316-0707-4aac-a5bf-e236a1010405 (old id 1406164)
date added to LUP
2009-06-05 11:09:28
date last changed
2016-04-16 10:06:14
@misc{dcac0316-0707-4aac-a5bf-e236a1010405,
  abstract     = {Kaposi's sarcoma-associated herpes virus (KSHV) encodes a complement inhibitor named KSHV complement control protein (KCP). We have previously shown that KCP inhibits the human complement system by disrupting the C3 convertase of complement. KCP can accelerate the decay of the classical C3 convertase and it can act as a cofactor for factor I (R), which then cleaves and inactivates C4b or C3b (in the classical and alternative convertase, respectively). The aim of this study was to 1) delineate the sites on KCP responsible for complement inhibition 2) study the binding of KCP to heparin and the surface of cells. We constructed a 3D model of the four CCP domains KCP by homology based modeling, which served as basis for site directed mutagenesis. A patch of positively charged amino acids in CCPI, stretching into CCP2 as well as a positive and a negative patch in the region between CCP2-3 were the most functionally important sites. KCP binds to heparin and the surface of cells via a site in CCPI.},
  author       = {Mark, Linda and Spiller, OB and Villoutreix, BO and Blom, AM},
  language     = {eng},
  pages        = {243--247},
  publisher    = {ARRAY(0xafcecc0)},
  series       = {Immunology 2004: Cytokine Network, Regulatory Cells, Signaling, and Apoptosis},
  title        = {Localization of functional sites in the viral complement inhibitor KCP},
  year         = {2004},
}