rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
2004-12-3
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pubmed:abstractText |
Cholesterol is believed to serve as the common receptor for the cholesterol-dependent cytolysins (CDCs). One member of this toxin family, Streptococcus intermedius intermedilysin (ILY), exhibits a narrow spectrum of cellular specificity that is seemingly inconsistent with this premise. We show here that ILY, via its domain 4 structure, binds to the glycosyl-phosphatidylinositol-linked membrane protein human CD59 (huCD59). CD59 is an inhibitor of the membrane attack complex of human complement. ILY specifically binds to huCD59 via residues that are the binding site for the C8alpha and C9 complement proteins. These studies provide a new model for the mechanism of cellular recognition by a CDC.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1545-9993
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1173-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15543155-Animals,
pubmed-meshheading:15543155-Antigens, CD59,
pubmed-meshheading:15543155-Bacterial Proteins,
pubmed-meshheading:15543155-Bacteriocins,
pubmed-meshheading:15543155-Binding Sites,
pubmed-meshheading:15543155-Cell Line,
pubmed-meshheading:15543155-Cholesterol,
pubmed-meshheading:15543155-Erythrocytes,
pubmed-meshheading:15543155-Glycosylation,
pubmed-meshheading:15543155-Humans,
pubmed-meshheading:15543155-Mice,
pubmed-meshheading:15543155-Models, Molecular,
pubmed-meshheading:15543155-Protein Structure, Tertiary,
pubmed-meshheading:15543155-Rabbits,
pubmed-meshheading:15543155-Substrate Specificity,
pubmed-meshheading:15543155-Trypsin
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pubmed:year |
2004
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pubmed:articleTitle |
Human CD59 is a receptor for the cholesterol-dependent cytolysin intermedilysin.
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pubmed:affiliation |
Microbiology and Immunology, The University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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