Staphylococcus aureus expresses a cell surface protein that binds both IgG and β2-glycoprotein I
L Zhang, K Jacobsson, K Ström, M Lindberg… - …, 1999 - microbiologyresearch.org
L Zhang, K Jacobsson, K Ström, M Lindberg, L Frykberg
Microbiology, 1999•microbiologyresearch.orgThe 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 β2-glycoprotein I (β2-GPI), also known as apolipoprotein H. The minimal β2-
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 …
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 β2-glycoprotein I (β2-GPI), also known as apolipoprotein H. The minimal β2-
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 …
Summary
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 β2-glycoprotein I (β2-GPI), also known as apolipoprotein H. The minimal β2-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 β2-GPI-binding activity, is expressed on the staphylococcal cell surface at levels varying between strains.
Microbiology Research