Linked Life Data

11371571

Source:http://linkedlifedata.com/resource/pubmed/id/11371571

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
2001-7-23
pubmed:abstractText
Staphylococcus epidermidis is an important opportunistic pathogen and is a major cause of foreign body infections. We have characterized the ligand binding activity of SdrG, a fibrinogen-binding microbial surface component recognizing adhesive matrix molecules from S. epidermidis. Western ligand blot analysis showed that a recombinant form of the N-terminal A region of SdrG bound to the native Bbeta chain of fibrinogen (Fg) and to a recombinant form of the Bbeta chain expressed in Escherichia coli. By analyzing recombinant truncates and synthetic peptide mimetics of the Fg Bbeta chain, the binding site for SdrG was localized to residues 6-20 of this polypeptide. Recombinant SdrG bound to a synthetic 25-amino acid peptide (beta1-25) representing the N terminus of the Fg Bbeta chain with a KD of 1.4 x 10(-7) m as determined by fluorescence polarization experiments. This was similar to the apparent K(D) (0.9 x 10(-7) m) calculated from an enzyme-linked immunosorbent assay where SdrG bound immobilized Fg in a concentration-dependent manner. SdrG could recognize fibrinopeptide B (residues 1-14), but with a substantially lower affinity than that observed for SdrG binding to synthetic peptides beta1-25 and beta6-20. However, SdrG does not bind to thrombin-digested Fg. Thus, SdrG appears to target the thrombin cleavage site in the Fg Bbeta chain. In fact, SdrG was found to inhibit thrombin-induced fibrinogen clotting by interfering with fibrinopeptide B release.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
276
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
27799-805
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11371571-Adhesins, Bacterial, pubmed-meshheading:11371571-Binding, Competitive, pubmed-meshheading:11371571-Binding Sites, pubmed-meshheading:11371571-Blotting, Western, pubmed-meshheading:11371571-Carrier Proteins, pubmed-meshheading:11371571-Cell Adhesion, pubmed-meshheading:11371571-DNA, Complementary, pubmed-meshheading:11371571-Dose-Response Relationship, Drug, pubmed-meshheading:11371571-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:11371571-Escherichia coli, pubmed-meshheading:11371571-Fibrinogen, pubmed-meshheading:11371571-Fibrinopeptide B, pubmed-meshheading:11371571-Kinetics, pubmed-meshheading:11371571-Ligands, pubmed-meshheading:11371571-Microscopy, Fluorescence, pubmed-meshheading:11371571-Peptides, pubmed-meshheading:11371571-Polymerase Chain Reaction, pubmed-meshheading:11371571-Protein Binding, pubmed-meshheading:11371571-Recombinant Fusion Proteins, pubmed-meshheading:11371571-Recombinant Proteins, pubmed-meshheading:11371571-Staphylococcus epidermidis, pubmed-meshheading:11371571-Thrombin
pubmed:year
2001
pubmed:articleTitle
SdrG, a fibrinogen-binding bacterial adhesin of the microbial surface components recognizing adhesive matrix molecules subfamily from Staphylococcus epidermidis, targets the thrombin cleavage site in the Bbeta chain.
pubmed:affiliation
Center for Extracellular Matrix Biology, Institute of Biosciences and Technology, Texas A & M University Health Science Center, Houston, Texas 77030-3303, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't