The response regulator Rrp2 is essential for the expression of major membrane lipoproteins in Borrelia burgdorferi

Xiaofeng F. Yang, Sophie M. Alani, Michael V. Norgard

Research output: Contribution to journalArticle

145 Citations (Scopus)

Abstract

Borrelia burgdorferi (Bb), the agent of Lyme disease, exists in nature through a complex enzootic life cycle that involves both ticks and mammals. As Bb transitions between its two diverse niches, profound adaptive changes occur that are reflected in differential patterns of gene expression, particularly involving lipoprotein genes. Using a mutagenesis approach, we show that Rrp2 (gene BB0763), one of the proteins predicted by the Bb genome (www.tigr.org) to be a response regulator of a two-component sensory transduction system, is a pivotal regulator governing the expression of major membrane lipoproteins such as OspC, DbpA, and MIp8, as well as many other mammalian infection-associated immunogens of Bb. Sequence analysis additionally suggested that Rrp2 is a bacterial enhancer-binding protein, essential for σ 54-dependent gene activation. Mutagenesis of a key amino acid residue within a putative activation domain revealed that Rrp2 controlled lipoprotein expression by governing the expression of the alternative σ-factor σs in a σ54-dependent manner. We therefore propose a signal transduction pathway involving Rrp2, σ 54, and σs, which in concert control the expression of key lipoproteins and other infection-associated immunogens in Bb.

Original languageEnglish (US)
Pages (from-to)11001-11006
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume100
Issue number19
DOIs
StatePublished - Sep 16 2003

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Borrelia burgdorferi
Lipoproteins
Membranes
Mutagenesis
Lyme Disease
Ticks
Infection
Life Cycle Stages
Transcriptional Activation
Genes
Sequence Analysis
Mammals
Signal Transduction
Carrier Proteins
Genome
Gene Expression
Amino Acids
Proteins

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

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abstract = "Borrelia burgdorferi (Bb), the agent of Lyme disease, exists in nature through a complex enzootic life cycle that involves both ticks and mammals. As Bb transitions between its two diverse niches, profound adaptive changes occur that are reflected in differential patterns of gene expression, particularly involving lipoprotein genes. Using a mutagenesis approach, we show that Rrp2 (gene BB0763), one of the proteins predicted by the Bb genome (www.tigr.org) to be a response regulator of a two-component sensory transduction system, is a pivotal regulator governing the expression of major membrane lipoproteins such as OspC, DbpA, and MIp8, as well as many other mammalian infection-associated immunogens of Bb. Sequence analysis additionally suggested that Rrp2 is a bacterial enhancer-binding protein, essential for σ 54-dependent gene activation. Mutagenesis of a key amino acid residue within a putative activation domain revealed that Rrp2 controlled lipoprotein expression by governing the expression of the alternative σ-factor σs in a σ54-dependent manner. We therefore propose a signal transduction pathway involving Rrp2, σ 54, and σs, which in concert control the expression of key lipoproteins and other infection-associated immunogens in Bb.",
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AU - Yang, Xiaofeng F.

AU - Alani, Sophie M.

AU - Norgard, Michael V.

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AB - Borrelia burgdorferi (Bb), the agent of Lyme disease, exists in nature through a complex enzootic life cycle that involves both ticks and mammals. As Bb transitions between its two diverse niches, profound adaptive changes occur that are reflected in differential patterns of gene expression, particularly involving lipoprotein genes. Using a mutagenesis approach, we show that Rrp2 (gene BB0763), one of the proteins predicted by the Bb genome (www.tigr.org) to be a response regulator of a two-component sensory transduction system, is a pivotal regulator governing the expression of major membrane lipoproteins such as OspC, DbpA, and MIp8, as well as many other mammalian infection-associated immunogens of Bb. Sequence analysis additionally suggested that Rrp2 is a bacterial enhancer-binding protein, essential for σ 54-dependent gene activation. Mutagenesis of a key amino acid residue within a putative activation domain revealed that Rrp2 controlled lipoprotein expression by governing the expression of the alternative σ-factor σs in a σ54-dependent manner. We therefore propose a signal transduction pathway involving Rrp2, σ 54, and σs, which in concert control the expression of key lipoproteins and other infection-associated immunogens in Bb.

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