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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1991-7-29
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pubmed:abstractText |
Human lactoferrin (HLf) is an iron-binding protein and a host-defence component at the mucosal surface. Recently, a specific receptor for HLf has been identified on a strain of Staphylococcus aureus associated with toxic shock syndrome. We have looked for the occurrence of 125I-HLf binding among 489 strains of S. aureus isolated from various clinical sources. HLf binding was common among S. aureus strains associated with furunculosis (94.3%), toxic shock syndrome (94.3%), endocarditis (83.3%) and septicaemia (82.8%) and other (nasal, vaginal or ocular) infections (96.1%) with a mean binding (in fmol) of 29.1, 21.9, 16.9, 22.2 and 29.2 respectively; the differences between mean HLf binding values of 29.1-29.2, 21.9-22.2 and 16.9 were significant. Furunculosis-associated (low-invasive or localised) isolates were high-to-moderate binders of HLf; 50% gave positive results at a threshold of greater than 31 fmol of 125I-HLf bound. In contrast, endocarditis-associated (high-invasive or systemic) isolates demonstrated low binding and did not bind 125I-HLf at the above threshold level. S. aureus recognised human or bovine Lf. However, bound 125I-HLf was more effectively inhibited in a dose-dependent manner by unlabelled bovine Lf than by homologous HLf. Binding of 125I-HLf to staphylococci was optimal with organisms grown in agar compared with those from broth cultures. The binding capacity of S. aureus was abolished when strains were grown on carbohydrate- and salt-rich agar media. HLf-binding ability of S. aureus did not correlate with fibronectin, fibrinogen, immunoglobulin G or laminin binding.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media,
http://linkedlifedata.com/resource/pubmed/chemical/Fibrinogen,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin G,
http://linkedlifedata.com/resource/pubmed/chemical/Lactoferrin,
http://linkedlifedata.com/resource/pubmed/chemical/Laminin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0022-2615
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
34
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
323-8
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:2056516-Culture Media,
pubmed-meshheading:2056516-Endocarditis,
pubmed-meshheading:2056516-Fibrinogen,
pubmed-meshheading:2056516-Fibronectins,
pubmed-meshheading:2056516-Furunculosis,
pubmed-meshheading:2056516-Immunoglobulin G,
pubmed-meshheading:2056516-Lactoferrin,
pubmed-meshheading:2056516-Laminin,
pubmed-meshheading:2056516-Sepsis,
pubmed-meshheading:2056516-Shock, Septic,
pubmed-meshheading:2056516-Staphylococcus aureus
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pubmed:year |
1991
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pubmed:articleTitle |
Human lactoferrin binding in clinical isolates of Staphylococcus aureus.
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pubmed:affiliation |
Department of Medical Microbiology, University of Lund, Malmö General Hospital, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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