Characterization of vitronectin-binding proteins of staphylococcus epidermidis

Staphylococcus epidermidis is the most common microorganism that is isolated from the cerebrospinal fluid (CSF) shunt infection patients. Vitronectin adsorbed on the surface of implants may mediate bacterial adhesion and colonization. To characterize vitronectin-binding properties, we analyzed S. ep...

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Bibliographic Details
Published in:Current microbiology 2001-05, Vol.42 (5), p.361-367
Main Authors: LI, Dai-Qing, LUNDBERG, Fredrik, LJUNGH, Asa
Format: Article
Language:English
Subjects:
Affinity chromatography
Amino acids
Autoradiography - methods
Bacterial diseases
Bacterial diseases of the urinary system
Bacterial Proteins - chemistry
Bacterial Proteins - isolation & purification
Bacterial Proteins - metabolism
Bacteriology
Biological and medical sciences
Cerebrospinal Fluid Shunts - adverse effects
Colonization
Culture media
DNA-Binding Proteins
Electrophoresis, Polyacrylamide Gel
Human bacterial diseases
Humans
Infectious diseases
Mass spectrometry
Medical sciences
Microbiology
Proteins
Staphylococcal Infections - microbiology
Staphylococcus epidermidis
Staphylococcus epidermidis - growth & development
Staphylococcus epidermidis - isolation & purification
Staphylococcus epidermidis - metabolism
Vitronectin - antagonists & inhibitors
Vitronectin - metabolism
vitronectin-binding protein
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Summary:Staphylococcus epidermidis is the most common microorganism that is isolated from the cerebrospinal fluid (CSF) shunt infection patients. Vitronectin adsorbed on the surface of implants may mediate bacterial adhesion and colonization. To characterize vitronectin-binding properties, we analyzed S. epidermidis BD5703 isolated from a CSF shunt infection. Expression of vitronectin-binding protein(s) depended on culture media. Two proteins (60 and 52 kDa) were purified from vitronectin affinity chromatography. Two other vitronectin-binding proteins (21 and 16 kDa) were purified from an ion-exchange column. All purified proteins blocked bacterial binding of immobilized vitronectin significantly except the 16-kDa protein. The N-terminal sequences of the 21- and 16-kDa proteins did not show any appreciable amino acid sequence homology. The 52-kDa protein was sequenced by mass spectrometry and identified as an autolysin. This report demonstrates that interaction of vitronectin with multiple recognition sites on BD5703 surface may contribute to bacterial colonization.
ISSN:0343-8651
1432-0991
DOI:10.1007/s002840010230