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Microbiology 155 (2009), 863-872; DOI  10.1099/mic.0.024604-0
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Microbiology 155 (2009), 863-872; DOI  10.1099/mic.0.024604-0
© 2009 Society for General Microbiology

The Borrelia burgdorferi outer-surface protein ErpX binds mammalian laminin

Catherine A. Brissette{dagger}, Ashutosh Verma{dagger}, Amy Bowman, Anne E. Cooley{ddagger} and Brian Stevenson

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.


Abbreviations: ECM, extracellular matrix

{dagger}These authors contributed equally to this work.

{ddagger}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.




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