Article
Binding characteristics of thrombin-activatable fibrinolysis inhibitor to streptococcal surface collagen-like proteins A and B.
Thrombosis and haemostasis - 1 Oct 2011
Valls Serón Mercedes, Plug Tom, Marquart J Arnoud, Marx Pauline F, Herwald Heiko, de Groot Philip G, Meijers Joost C M
Abstract excerpt
Streptococcus pyogenes is the causative agent in a wide range of diseases in humans. Thrombin-activatable fibrinolysis inhibitor (TAFI) binds to collagen-like proteins SclA and SclB at the surface of S. pyogenes. Activation of TAFI at this surface redirects inflammation from a transient to chronic state by modulation of the kallikrein/kinin system. We investigated TAFI binding characteristics to SclA/SclB....
Topics
- Amino Acid Sequence
- Bacterial Proteins
- Blood Coagulation Disorders
- Carboxypeptidase B2
- Enzyme Activation
- Exotoxins
- Humans
- Membrane Proteins
- Molecular Sequence Data
- Mutation
- Peptide Fragments
- Protein Binding
- Protein Stability
- Streptococcal Infections