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Department of Microbiology, Immunology, and Molecular Genetics, University of Kentucky College of Medicine, Lexington, KY 40536-0298, USA
Correspondence
Brian Stevenson
brian.stevenson{at}uky.edu
The Lyme disease spirochaete, Borrelia burgdorferi, can invade and persistently infect its hosts' connective tissues. We now demonstrate that B. burgdorferi adheres to the extracellular matrix component laminin. The surface-exposed outer-membrane protein ErpX was identified as having affinity for laminin, and is the first laminin-binding protein to be identified in a Lyme disease spirochaete. The adhesive domain of ErpX was shown to be contained within a small, unstructured hydrophilic segment at the protein's centre. The sequence of that domain is distinct from any previously identified bacterial laminin adhesin, suggesting a unique mode of laminin binding.
These authors contributed equally to this work.
Present address: Department of Surgery, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.
A supplementary sequence alignment is available with the online version of this paper.
This article has been cited by other articles:
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A. Verma, C. A. Brissette, A. Bowman, and B. Stevenson Borrelia burgdorferi BmpA Is a Laminin-Binding Protein Infect. Immun., November 1, 2009; 77(11): 4940 - 4946. [Abstract] [Full Text] [PDF] |
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C. A. Brissette, T. Bykowski, A. E. Cooley, A. Bowman, and B. Stevenson Borrelia burgdorferi RevA Antigen Binds Host Fibronectin Infect. Immun., July 1, 2009; 77(7): 2802 - 2812. [Abstract] [Full Text] [PDF] |
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