Lyme borreliosis spirochete Erp proteins, their known host ligands, and potential roles in mammalian infection

Catherine A. Brissette, Anne E. Cooley, Logan H. Burns, Sean P. Riley, Ashutosh Verma, Michael E. Woodman, Tomasz Bykowski, Brian Stevenson

Research output: Contribution to journalShort surveypeer-review

42 Scopus citations

Abstract

Lyme borreliae naturally maintain numerous distinct DNA elements of the cp32 family, each of which carries a mono- or bicistronic erp locus. The encoded Erp proteins are surface-exposed outer membrane lipoproteins that are produced at high levels during mammalian infection but largely repressed during colonization of vector ticks. Recent studies have revealed that some Erp proteins can serve as bacterial adhesins, binding host proteins such as the complement regulator factor H and the extracellular matrix component laminin. These results suggest that Erp proteins play roles in multiple aspects of mammalian infection.

Original languageEnglish
Pages (from-to)257-267
Number of pages11
JournalInternational Journal of Medical Microbiology
Volume298
Issue numberSUPPL. 1
DOIs
StatePublished - Sep 1 2008

Bibliographical note

Funding Information:
Research on Erp proteins by our laboratory is funded by US National Institutes of Health Grant R01-AI44245. We thank our many colleagues around the world for their helpful scientific discussions and debates.

Keywords

  • Adhesin
  • Borrelia burgdorferi
  • Complement
  • Factor H
  • Laminin
  • Outer surface protein

ASJC Scopus subject areas

  • Microbiology
  • Microbiology (medical)
  • Infectious Diseases

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