Linked Life Data

19388165

Source:http://linkedlifedata.com/resource/pubmed/id/19388165

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2009-4-23
pubmed:abstractText
Complement activation and resulting opsonisation with C3b form key arms of the innate immune defense against infections. However, a wide variety of pathogens subvert complement attack by binding host complement inhibitors, which results in diminished opsonophagocytosis and killing of bacteria by lysis. Human C4b-binding protein (C4BP) binds Neisseria gonorrhoeae and Streptococcus pyogenes, both uniquely human pathogens. This binding specificity is circumvented by other bacterial species, which bind C4BP from numerous mammalian hosts that they infect. Binding of C4BP to Neisseria is mediated by outer membrane porin proteins and appears to be one of the main factors mediating serum resistance. Targeting C4BP binding sites on bacterial surfaces with vaccine-induced antibodies may block binding of C4BP and enhance a common vaccine design strategy that depends on the generation of complement-dependent bactericidal and opsonophagocytic antibody activities.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0264-410X
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
26 Suppl 8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
I49-55
pubmed:dateRevised
2011-4-7
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Contribution of interactions between complement inhibitor C4b-binding protein and pathogens to their ability to establish infection with particular emphasis on Neisseria gonorrhoeae.
pubmed:affiliation
Lund University, Department of Laboratory Medicine, Division of Medical Protein Chemistry, University Hospital Malmö entrance 46, The Wallenberg Laboratory floor 4, S-205 02 Malmö, Sweden. Anna.Blom@med.lu.se
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural