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Fibrinogen fragment D is necessary and sufficient to anchor a surface plasminogen‐activating complex in Streptococcus pyogenes
Author(s) -
Hess Jennifer L.,
Boyle Michael D. P.
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200500189
Subject(s) - streptococcus pyogenes , fibrinogen , fragment (logic) , microbiology and biotechnology , chemistry , biology , computational biology , bacteria , biochemistry , genetics , computer science , staphylococcus aureus , algorithm
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.