Abstract
The existence of a second IgG-binding protein, protein Sbi, in Staphylococcus aureus has been reported previously. Later data indicated that protein Sbi also bound another serum component. This component has now been affinity-purified on immobilized protein Sbi and identified as beta2-glycoprotein I (beta2-GPI), also known as apolipoprotein H. The minimal beta2-GPI-binding domain was identified by shotgun phage display and the binding was shown to be mediated by a region of 57 amino acids, clearly separated from the IgG-binding domain. It is also shown that protein Sbi, and thus the beta2-GPI-binding activity, is expressed on the staphylococcal cell surface at levels varying between strains.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Bacterial Proteins*
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Bacteriophages / genetics
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Binding Sites
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Blotting, Western
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Carrier Proteins / analysis
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Carrier Proteins / chemistry
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Chromatography, Affinity
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Glycoproteins / blood
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Glycoproteins / chemistry
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Glycoproteins / isolation & purification
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Glycoproteins / metabolism*
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Humans
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Immunoglobulin G / metabolism*
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Membrane Proteins / analysis
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Membrane Proteins / chemistry
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Membrane Proteins / metabolism*
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Molecular Sequence Data
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Peptide Library
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Protein Binding
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Staphylococcus aureus / chemistry
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Staphylococcus aureus / metabolism*
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beta 2-Glycoprotein I
Substances
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Bacterial Proteins
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Carrier Proteins
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Glycoproteins
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Immunoglobulin G
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Membrane Proteins
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Peptide Library
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Sbi protein, Staphylococcus aureus
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beta 2-Glycoprotein I