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.

Abstract

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

Substances

  • Bacterial Outer Membrane Proteins
  • Laminin
  • Recombinant Proteins