ArticleMolecular microbiology2013
The HtrA protease of Borrelia burgdorferi degrades outer membrane protein BmpD and chemotaxis phosphatase CheX.
Article in Molecular microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
36 citing papers in PubMed, 52 citations in OpenAlex.
- Leptospira interrogans HtrA protease is a potent inducer of multifaceted cellular responses.Antonie van Leeuwenhoek · 2026Article
- Efficient resuscitation of early-stage viable but non-culturable cells ofApplied and environmental microbiology · 2026Article
- Altering chemotaxis as a strategy to enhance the foraging range of motility-restricted bacteria.Communications biology · 2026Article
- Borrelia burgdorferi serine protease HtrA is a pleiotropic regulator of stress response, motility, flagellar hemostasis, and infectivity.Communications biology · 2025Article
- Dual roles for a tick protein disulfide isomerase during the life cycle of the Lyme disease agent.mBio · 2024Article
- Investigating the role of aFrontiers in oral health · 2024Article
- Pathogenicity and virulence ofVirulence · 2023Review
- A chemosensory-like histidine kinase is dispensable for chemotaxis in vitro but regulates the virulence of Borrelia burgdorferi through modulating the stability of RpoS.PLoS pathogens · 2023Article
- BB0761, a MepM homolog, contributes to Borrelia burgdorferi cell division and mammalian infectivity.Molecular microbiology · 2022Article
- Controlled Proteolysis of an Essential Virulence Determinant Dictates Infectivity of Lyme Disease Pathogens.Infection and immunity · 2022Article
- Endogenous and Borrowed Proteolytic Activity in theMicrobiology and molecular biology reviews : MMBR · 2021Review
- Article
- Lyme Disease Pathogenesis.Current issues in molecular biology · 2021Review
- Host-specific functional compartmentalization within the oligopeptide transporter during the Borrelia burgdorferi enzootic cycle.PLoS pathogens · 2021Article
- The Lon-1 Protease Is Required by Borrelia burgdorferi To Infect the Mammalian Host.Infection and immunity · 2020Article
- Analysis of a flagellar filament cap mutant reveals that HtrA serine protease degrades unfolded flagellin protein in the periplasm of Borrelia burgdorferi.Molecular microbiology · 2019Article
- Protein Secretion in Spirochetes.Microbiology spectrum · 2019Article
- Protease Activity ofFrontiers in cellular and infection microbiology · 2019Article
- Assessing the Contribution of an HtrA Family Serine Protease DuringFrontiers in cellular and infection microbiology · 2019Article
- Proteolysis of histidine kinase VgrS inhibits its autophosphorylation and promotes osmostress resistance in Xanthomonas campestris.Nature communications · 2018Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Borrelia burgdorferi, the spirochaetal agent of Lyme disease, codes for a single HtrA protein, HtrABb (BB0104) that is homologous to DegP of Escherichia coli (41% amino acid identity). HtrABb shows physical and biochemical similarities to DegP in that it has the trimer as its fundamental unit and can degrade casein via its catalytic serine. Recombinant HtrABb exhibits proteolytic activity in vitro, while a mutant (HtrABbS198A) does not. However, HtrABb and DegP have some important differences as well. Native HtrABb occurs in both membrane-bound and soluble forms. Despite its homology to DegP, HtrABb could not complement an E. coli DegP deletion mutant. Late stage Lyme disease patients, as well as infected mice and rabbits developed a robust antibody response to HtrABb, indicating that it is a B-cell antigen. In co-immunoprecipitation studies, a number of potential binding partners for HtrABb were identified, as well as two specific proteolytic substrates, basic membrane protein D (BmpD/BB0385) and chemotaxis signal transduction phosphatase CheX (BB0671). HtrABb may function in regulating outer membrane lipoproteins and in modulating the chemotactic response of B. burgdorferi.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.