An inverted repeat in the ospC operator is required for induction in Borrelia burgdorferi

Borrelia burgdorferi, the spirochete that causes Lyme disease, differentially regulates synthesis of the outer membrane lipoprotein OspC to infect its host. OspC is required to establish infection but then repressed in the mammal to avoid clearance by the adaptive immune response. Inverted repeats (...

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Bibliographic Details
Published in:PloS one 2013-07, Vol.8 (7), p.e68799
Main Authors: Drecktrah, Dan, Hall, Laura S, Hoon-Hanks, Laura L, Samuels, D Scott
Format: Article
Language:English
Subjects:
Adaptive immunity
Antigens, Bacterial - chemistry
Antigens, Bacterial - genetics
Arachnids
Bacterial Outer Membrane Proteins - chemistry
Bacterial Outer Membrane Proteins - genetics
Base Sequence
Biology
Borrelia burgdorferi
Borrelia burgdorferi - genetics
Borrelia burgdorferi - metabolism
Deoxyribonucleic acid
DNA
DNA biosynthesis
DNA, Bacterial - genetics
DNA, Bacterial - metabolism
E coli
Escherichia coli
Experiments
Gene expression
Gene Expression Regulation, Bacterial
Gene Order
Genomes
Health aspects
Immune clearance
Immune response
Immune system
Infection
Infections
Inverted repeat
Inverted Repeat Sequences
Lyme disease
Mammals
Medicine
Molecular Sequence Data
Nucleotide sequence
Operator Regions, Genetic
pH effects
Plasmids
Protein Biosynthesis
Proteins
Site-directed mutagenesis
Spirochetes
Studies
Supercoiling
Synthesis
Temperature
Vector-borne diseases
Virulence
Virulence factors
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Description
Summary:Borrelia burgdorferi, the spirochete that causes Lyme disease, differentially regulates synthesis of the outer membrane lipoprotein OspC to infect its host. OspC is required to establish infection but then repressed in the mammal to avoid clearance by the adaptive immune response. Inverted repeats (IR) upstream of the promoter have been implicated as an operator to regulate ospC expression. We molecularly dissected the distal inverted repeat (dIR) of the ospC operator by site-directed mutagenesis at its endogenous location on the circular plasmid cp26. We found that disrupting the dIR but maintaining the proximal IR prevented induction of OspC synthesis by DNA supercoiling, temperature, and pH. Moreover, the base-pairing potential of the two halves of the dIR was more important than the nucleotide sequence in controlling OspC levels. These results describe a cis-acting element essential for the expression of the virulence factor OspC.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0068799