The Borrelia burgdorferi outer-surface protein ErpX binds mammalian laminin

Microbiology. 2009 Mar;155(Pt 3):863-872. doi: 10.1099/mic.0.024604-0.


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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacterial Outer Membrane Proteins / genetics
  • Bacterial Outer Membrane Proteins / metabolism*
  • Binding Sites
  • Borrelia burgdorferi / genetics
  • Borrelia burgdorferi / metabolism*
  • Laminin / metabolism*
  • Mice
  • Molecular Sequence Data
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism


  • Bacterial Outer Membrane Proteins
  • Laminin
  • Recombinant Proteins