ArticleThe Journal of infectious diseases2015
BB0323 and novel virulence determinant BB0238: Borrelia burgdorferi proteins that interact with and stabilize each other and are critical for infectivity.
Article in The Journal of infectious diseases, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed, 32 citations in OpenAlex.
- Protective efficacy of mutant strains ofInfection and immunity · 2026Article
- Targeting of interaction between BB0323-BB0238 informs new paradigms in Lyme disease therapeutics.PLoS pathogens · 2026Article
- Assessment of the hypothetical protein BB0616 in the murine infection ofInfection and immunity · 2024Article
- A systemic approach to identify non-abundant immunogenic proteins in Lyme disease pathogens.mSystems · 2024Article
- 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
- Controlled Proteolysis of an Essential Virulence Determinant Dictates Infectivity of Lyme Disease Pathogens.Infection and immunity · 2022Article
- FliL ring enhances the function of periplasmic flagella.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Application of temperature-responsive HIS-tag fluorophores to differential scanning fluorimetry screening of small molecule libraries.Frontiers in pharmacology · 2022Article
- Article
- Borrelia peptidoglycan interacting Protein (BpiP) contributes to the fitness of Borrelia burgdorferi against host-derived factors and influences virulence in mouse models of Lyme disease.PLoS pathogens · 2021Article
- BB0259 Encompasses a Peptidoglycan Lytic Enzyme Function for Proper Assembly of Periplasmic Flagella inFrontiers in microbiology · 2021Article
- Lyme Disease Pathogenesis.Current issues in molecular biology · 2021Review
- Serologic Evidence for the Exposure of Eastern Coyotes (mSphere · 2020Article
- Mutation of the Carboxy-Terminal Processing Protease inPathogens (Basel, Switzerland) · 2020Article
- BB0326 is responsible for the formation of periplasmic flagellar collar and assembly of the stator complex in Borrelia burgdorferi.Molecular microbiology · 2020Article
- Membrane directed expression in Escherichia coli of BBA57 and other virulence factors from the Lyme disease agent Borrelia burgdorferi.Scientific reports · 2019Article
- Borrelia burgdorferi protein interactions critical for microbial persistence in mammals.Cellular microbiology · 2019Review
- A tetratricopeptide repeat domain protein has profound effects on assembly of periplasmic flagella, morphology and motility of the lyme disease spirochete Borrelia burgdorferi.Molecular microbiology · 2018Article
- Borrelia burgdorferi surface-located Lmp1 protein processed into region-specific polypeptides that are critical for microbial persistence.Cellular microbiology · 2018Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
We have shown that Borrelia burgdorferi gene product BB0323 is essential for cell fission and pathogen persistence in vivo. Here we describe characterization of a conserved hypothetical protein annotated as BB0238, which specifically interacts with the N-terminal region of BB0323. We show that BB0238 is a subsurface protein, and similar to BB0323, exists in the periplasm and as a membrane-bound protein. Deletion of bb0238 in infectious B. burgdorferi did not affect microbial growth in vitro or survival in ticks, but the mutant was unable to persist in mice or transmit from ticks--defects that are restored on genetic complementation. Remarkably, BB0238 and BB0323 contribute to mutual posttranslational stability, because deletion of one causes dramatic reduction in the protein level of the other partner. Interference with the function of BB0238 or BB0323 and their interaction may provide novel strategies to combat B. burgdorferi infection.
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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.