Differential binding of host complement inhibitor factor H by Borrelia burgdorferi Erp surface proteins: A possible mechanism underlying the expansive host range of Lyme disease spirochetes

Brian Stevenson, Nazira El-Hage, Melissa A. Hines, Jennifer C. Miller, Kelly Babb

Research output: Contribution to journalArticlepeer-review

193 Scopus citations

Abstract

The Lyme disease spirochete, Borrelia burgdorferi, is capable of infecting a wide variety of vertebrates. This broad host range implies that B. burgdorferi possesses the ability to contravene the immune defenses of many potential hosts. B. burgdorferi produces multiple different Erp proteins on its outer membrane during mammalian infection. It was reported previously that one Erp protein can bind human factor H (J. Hellwage, T. Meri, T. Heikkilä, A. Alitalo, J. Panelius, P. Lahdenne, I. J. T. Seppälä, and S. Meri, J. Biol. Chem. 276:8427-8435, 2001). In this paper we report that the ability to bind the complement inhibitor factor H is a general characteristic of Erp proteins. Furthermore, each Erp protein exhibits different relative affinities for the complement inhibitors of various potential animal hosts. The data suggest that the presence of multiple Erp proteins on the surface can allow a single B. burgdorferi bacterium to resist complement-mediated killing in any of the wide range of potential hosts that it might infect. Thus, Erp proteins likely contribute to the persistence of B. burgdorferi in nature and to the ability of this bacterium to cause Lyme disease in humans and other animals.

Original languageEnglish
Pages (from-to)491-497
Number of pages7
JournalInfection and Immunity
Volume70
Issue number2
DOIs
StatePublished - 2002

ASJC Scopus subject areas

  • Parasitology
  • Microbiology
  • Immunology
  • Infectious Diseases

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