You are not currently logged in.
Access JSTOR through your library or other institution:
Complement Regulator—Acquiring Surface Protein 1 of Borrelia burgdorferi Binds to Human Bone Morphogenic Protein 2, Several Extracellular Matrix Proteins, and Plasminogen
Teresia Hallström, Katrin Haupt, Peter Kraiczy, Peter Hortschansky, Reinhard Wallich, Christine Skerka and Peter F. Zipfel
The Journal of Infectious Diseases
Vol. 202, No. 3 (1 August 2010), pp. 490-498
Published by: Oxford University Press
Stable URL: http://www.jstor.org/stable/25706944
Page Count: 9
You can always find the topics here!Topics: Proteins, Membrane proteins, Collagens, Physiological regulation, Borrelia burgdorferi, Infections, Pathogens, Polyclonal antibodies, Borrelia, Monoclonal antibodies
Were these topics helpful?See something inaccurate? Let us know!
Select the topics that are inaccurate.
Preview not available
Lyme disease—causing Borrelia burgdorferi spirochetes express up to 5 complement regulator—acquiring surface proteins (CRASPs). To better define how CRASP-1 contributes to infection, we aimed to identify novel CRASP-1—binding host proteins. Here, we identified a number of novel human CRASP-1—binding proteins, including bone morphogenic protein 2, collagen I, collagen III, collagen IV, fibronectin, laminin, and plasminogen. The plasminogen-binding regions were located in 2 separate regions of CRASP-1. Our results demonstrated that plasminogen-bound CRASP-1 can be converted to plasmin by the urokinase-type plasminogen activator and that proteolytically active plasmin cleaves the synthetic chromogenic substrate S-2251 and the natural substrate fibrinogen. In conclusion, CRASP-1 is a multifunctional protein of B. burgdorferi that binds to several human extracellular matrix proteins and plasminogen. These interactions may contribute to adhesion, bacterial colonization, and organ tropism and may allow dissemination of B. burgdorferi in the host.
The Journal of Infectious Diseases © 2010 Oxford University Press