title: Fibrinogen fragment D is necessary and sufficient to anchor a surface plasminogen-activating complex in Streptococcus pyogenes.
abstract: In this study, the importance of different domains of the fibrinogen molecule in the binding and assembly of a surface plasminogen (plgn) activator has been analyzed. This was achieved using SELDI technology that enabled dissociation of bound fragments from intact bacteria and accurate distinction between fibrinogen fragments based on their molecular mass. These studies indicate that Streptococcus pyogenes binds directly to human fibrinogen fragment D but not fragment E. The predominant surface proteins binding to fragment D were associated with the mrp gene product. Surface-associated fibrinogen fragment D was capable of anchoring a functional surface plgn activator complex. Taken together, these data indicated that fragment D of fibrinogen is necessary and sufficient to anchor a plgn activator complex on the surface of Streptococcus pyogenes.
authors.affiliation: Department of Biology, Juniata College, 1700 Moore Street, Huntingdon, PA 16652, USA.
authors.forename: Jennifer L
authors.initials: JL
authors.lastname: Hess
authors.forename: Michael D P
authors.initials: MD
authors.lastname: Boyle
mesh_terms: D005338:Fibrin Fibrinogen Degradation Products / Q000502:physiology*; D010958:Plasminogen / Q000378:metabolism*; D011485:Protein Binding; D013297:Streptococcus pyogenes / Q000737:chemistry* / Q000378:metabolism
chemical_list: D005338:Fibrin Fibrinogen Degradation Products; C015214:fibrinogen D fragment; D010958:Plasminogen