Affiliation:
1. Department of Microbiology, Immunology, and Molecular Genetics, University of Kentucky College of Medicine, Lexington, Kentucky 40536-0298
2. Department of Chemistry, University of Kentucky, Lexington, Kentucky 40536-0055
Abstract
ABSTRACT
All examined isolates of the Lyme disease spirochete,
Borrelia burgdorferi
, naturally maintain numerous variants of a prophage family as circular cp32 episomes. Each cp32 carries a locus encoding one or two different Erp outer membrane, surface-exposed lipoproteins. Many of the Erp proteins bind a host complement regulator, factor H, which is hypothesized to protect the spirochete from complement-mediated killing. We now describe the isolation and characterization of a novel, chromosomally encoded protein, EbfC, that binds specific DNA sequences located immediately 5′ of all
erp
loci. This is one of the first site-specific DNA-binding proteins to be identified in any spirochete. The location of the
ebfC
gene on the
B. burgdorferi
chromosome suggests that the cp32 prophages have evolved to use this bacterial host protein for their own benefit and that EbfC probably plays additional roles in the bacterium. A wide range of other bacteria encode homologs of EbfC, none of which have been well characterized, so demonstration that
B. burgdorferi
EbfC is a site-specific DNA-binding protein has broad implications across the eubacterial kingdom.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
39 articles.
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