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Kaposi's sarcoma-associated herpes virus complement control protein: KCP - complement inhibition and more.

Mark, Linda LU ; Spiller, O Brad; Villoutreix, Bruno O and Blom, Anna LU (2007) In Molecular Immunology 44. p.11-22
Abstract
The complement system is an important part of innate immunity providing immediate protection against pathogens without a need for previous exposure, as well as priming the adaptive immune response through opsonisation, leukocyte recruitment and enhancing humoral immune responses. Its importance is not only shown through recurring fulminant infections in individuals with complement component deficiencies, but also through the many complement evasion strategies discovered for a wide range of infectious microbes (including acquisition of endogenous host complement inhibitors and expression of own homologues). Knowledge of these mechanisms at a molecular level may aid development of vaccines and novel therapeutic strategies. Here, we review... (More)
The complement system is an important part of innate immunity providing immediate protection against pathogens without a need for previous exposure, as well as priming the adaptive immune response through opsonisation, leukocyte recruitment and enhancing humoral immune responses. Its importance is not only shown through recurring fulminant infections in individuals with complement component deficiencies, but also through the many complement evasion strategies discovered for a wide range of infectious microbes (including acquisition of endogenous host complement inhibitors and expression of own homologues). Knowledge of these mechanisms at a molecular level may aid development of vaccines and novel therapeutic strategies. Here, we review the structure-function studies of the membrane-bound complement inhibitor KCP that is expressed on the surface of Kaposi's sarcoma-associated herpesvirus (KSHV) virions and infected cells. KCP accelerates the decay of classical C3 convertase and induces the degradation of activated complement factors C4b and C3b by serine proteinase, factor I. Molecular modeling and site-directed mutagenesis have identified sites on the surface of endogenous human inhibitors. KCP additionally enhances virion binding to permissive cells through a heparin/heparan sulfate-binding site located at the N-terminus of the protein. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Molecular Immunology
volume
44
pages
11 - 22
publisher
Pergamon
external identifiers
  • wos:000241408400003
  • scopus:33750487181
ISSN
1872-9142
DOI
10.1016/j.molimm.2006.06.018
language
English
LU publication?
yes
id
70d73ee3-bf25-46c9-84c2-2be911825045 (old id 160118)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=16905191&dopt=Abstract
date added to LUP
2007-07-26 08:40:24
date last changed
2017-01-01 06:50:56
@article{70d73ee3-bf25-46c9-84c2-2be911825045,
  abstract     = {The complement system is an important part of innate immunity providing immediate protection against pathogens without a need for previous exposure, as well as priming the adaptive immune response through opsonisation, leukocyte recruitment and enhancing humoral immune responses. Its importance is not only shown through recurring fulminant infections in individuals with complement component deficiencies, but also through the many complement evasion strategies discovered for a wide range of infectious microbes (including acquisition of endogenous host complement inhibitors and expression of own homologues). Knowledge of these mechanisms at a molecular level may aid development of vaccines and novel therapeutic strategies. Here, we review the structure-function studies of the membrane-bound complement inhibitor KCP that is expressed on the surface of Kaposi's sarcoma-associated herpesvirus (KSHV) virions and infected cells. KCP accelerates the decay of classical C3 convertase and induces the degradation of activated complement factors C4b and C3b by serine proteinase, factor I. Molecular modeling and site-directed mutagenesis have identified sites on the surface of endogenous human inhibitors. KCP additionally enhances virion binding to permissive cells through a heparin/heparan sulfate-binding site located at the N-terminus of the protein.},
  author       = {Mark, Linda and Spiller, O Brad and Villoutreix, Bruno O and Blom, Anna},
  issn         = {1872-9142},
  language     = {eng},
  pages        = {11--22},
  publisher    = {Pergamon},
  series       = {Molecular Immunology},
  title        = {Kaposi's sarcoma-associated herpes virus complement control protein: KCP - complement inhibition and more.},
  url          = {http://dx.doi.org/10.1016/j.molimm.2006.06.018},
  volume       = {44},
  year         = {2007},
}