title: Ig-binding bacterial proteins also bind proteinase inhibitors.
abstract: Protein G is a streptococcal cell wall protein with separate binding sites for IgG and human serum albumin (HSA). In the present work it was demonstrated that alpha 2-macroglobulin (alpha 2M) and kininogen, two proteinase inhibitors of human plasma, bound to protein G, whereas 23 other human proteins showed no affinity. alpha 2M was found to interact with the IgG-binding domains of protein G, and in excess alpha 2M inhibited IgG binding and vice versa. A synthetic peptide, corresponding to one of the homologous IgG-binding domains of protein G, blocked binding of protein G to alpha 2M. Protein G showed affinity for both native and proteinase complexed alpha 2M but did not bind to the reduced form of alpha 2M, or to the C-terminal domain of the protein known to interact with alpha 2M receptors on macrophages. Binding of protein G to alpha 2M and kininogen did not interfere with their inhibitory activity on proteinases, and the interaction between protein G and the two proteinase inhibitors was not due to proteolytic activity of protein G. The finding that protein G has affinity for proteinase inhibitors was generalized to comprise also other Ig binding bacterial proteins. Thus, alpha 2M and kininogen, were shown to bind both protein A of Staphylococcus aureus and protein L of Peptococcus magnus. The results described above suggest that Ig-binding proteins are involved in proteolytic events, which adds a new and perhaps functional aspect to these molecules.
authors: Department of Medical Microbiology, University of Lund, Sweden.
authors: U
authors: U
authors: Sjöbring
authors: J
authors: J
authors: Trojnar
authors: A
authors: A
authors: Grubb
authors: B
authors: B
authors: Akerström
authors: L
authors: L
authors: Björck
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism*; D066298:In Vitro Techniques; D007704:Kininogens / Q000378:metabolism; D008222:Lymphokines / Q000378:metabolism*; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000378:metabolism; D029584:Prostatic Secretory Proteins; D011480:Protease Inhibitors / Q000378:metabolism*; D011485:Protein Binding; D013291:Streptococcus; D014357:Trypsin / Q000378:metabolism; D000511:alpha-Macroglobulins / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; C029152:G-substrate; D007704:Kininogens; D008222:Lymphokines; D009419:Nerve Tissue Proteins; D029584:Prostatic Secretory Proteins; D011480:Protease Inhibitors; D000511:alpha-Macroglobulins; C043076:beta-microseminoprotein; C013059:immunoglobulin-binding factors; D014357:Trypsin