Linked Life Data

9703988

Source:http://linkedlifedata.com/resource/pubmed/id/9703988

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-9-8
pubmed:abstractText
Staphylococcus aureus produces and secretes a protein, Efb, that binds to fibrinogen, seems to be required for virulence, and may benefit the microorganism by delaying wound healing. Interactions of Efb with fibrinogen are influenced by divalent metal cations, including Ca2+. Increasing concentrations of Ca2+ increased the binding of fibrinogen to immobilized Efb, whereas binding of Efb to immobilized fibrinogen was decreased with increasing Ca2+ concentration. Studies with synthetic peptides showed that peptides from the carboxyl terminal half of Efb bound to soluble fibrinogen and enhanced the binding of fibrinogen to Efb. A peptide corresponding to a repeated sequence in the amino terminal half of the protein also bound fibrinogen and inhibited binding of fibrinogen to Efb. These results may provide clues to the biological function of Efb and aid in the rational design of agents to block the Efb fibrinogen interaction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
248
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
690-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Identification of functional domains in Efb, a fibrinogen binding protein of Staphylococcus aureus.
pubmed:affiliation
Department of Immunology, Microbiology, Pathology, and Infectious Diseases, Huddinge Hospital, Karolinska Institute, Sweden. david.wade@impi.ki.se
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't