ArticleInfection and immunity2016
HtrA, a Temperature- and Stationary Phase-Activated Protease Involved in Maturation of a Key Microbial Virulence Determinant, Facilitates Borrelia burgdorferi Infection in Mammalian Hosts.
Article in Infection and immunity, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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
30 citing papers in PubMed, 42 citations in OpenAlex.
- Leptospira interrogans HtrA protease is a potent inducer of multifaceted cellular responses.Antonie van Leeuwenhoek · 2026Article
- Targeting of interaction between BB0323-BB0238 informs new paradigms in Lyme disease therapeutics.PLoS pathogens · 2026Article
- Heterologous Expression, Purification, and Characterization of a High-Temperature Requirement A (HtrA) Protease Homologue from Leptospira.Applied biochemistry and biotechnology · 2025Article
- Article
- Borrelia burgdorferi serine protease HtrA is a pleiotropic regulator of stress response, motility, flagellar hemostasis, and infectivity.Communications biology · 2025Article
- HtrA3 paves the way for MSC migration and promotes osteogenesis.Bioactive materials · 2024Article
- A systemic approach to identify non-abundant immunogenic proteins in Lyme disease pathogens.mSystems · 2024Article
- 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
- Dome1-JAK-STAT signaling between parasite and host integrates vector immunity and development.Science (New York, N.Y.) · 2023Article
- Application of biophysical methods for improved protein production and characterization: A case study on an high-temperature requirement A-family bacterial protease.Protein science : a publication of the Protein Society · 2022Article
- Dual role of an essential HtrA2/Omi protease in the human malaria parasite: Maintenance of mitochondrial homeostasis and induction of apoptosis-like cell death under cellular stress.PLoS pathogens · 2022Article
- 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
- Application of temperature-responsive HIS-tag fluorophores to differential scanning fluorimetry screening of small molecule libraries.Frontiers in pharmacology · 2022Article
- Endogenous and Borrowed Proteolytic Activity in theMicrobiology and molecular biology reviews : MMBR · 2021Review
- Article
- Lyme Disease Pathogenesis.Current issues in molecular biology · 2021Review
- The Lon-1 Protease Is Required by Borrelia burgdorferi To Infect the Mammalian Host.Infection and immunity · 2020Article
- A joint effort: The interplay between the innate and the adaptive immune system in Lyme arthritis.Immunological reviews · 2020Review
- Characterization of 6S RNA in the Lyme disease spirochete.Molecular microbiology · 2020Article
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Authors and funding
11 authors at 6 institutions in 3 countries.
Funding
Abstract
High-temperature requirement protease A (HtrA) represents a family of serine proteases that play important roles in microbial biology. Unlike the genomes of most organisms, that of Borrelia burgdorferi notably encodes a single HtrA gene product, termed BbHtrA. Previous studies identified a few substrates of BbHtrA; however, their physiological relevance could not be ascertained, as targeted deletion of the gene has not been successful. Here we show that BbhtrA transcripts are induced during spirochete growth either in the stationary phase or at elevated temperature. Successful generation of a BbhtrA deletion mutant and restoration by genetic complementation suggest a nonessential role for this protease in microbial viability; however, its remarkable growth, morphological, and structural defects during cultivation at 37°C confirm a high-temperature requirement for protease activation and function. The BbhtrA-deficient spirochetes were unable to establish infection of mice, as evidenced by assessment of culture, PCR, and serology. We show that transcript abundance as well as proteolytic processing of a borrelial protein required for cell fission and infectivity, BB0323, is impaired in BbhtrA mutants grown at 37°C, which likely contributed to their inability to survive in a mammalian host. Together, these results demonstrate the physiological relevance of a unique temperature-regulated borrelial protease, BbHtrA, which further enlightens our knowledge of intriguing aspects of spirochete biology and infectivity.
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