ArticleMolecular microbiology2013
Proteolysis of BB0323 results in two polypeptides that impact physiologic and infectious phenotypes in Borrelia burgdorferi.
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 31 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
31 citing papers in PubMed, 45 citations in OpenAlex.
- Targeting of interaction between BB0323-BB0238 informs new paradigms in Lyme disease therapeutics.PLoS pathogens · 2026Article
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- A Borrelia burgdorferi LptD homolog is required for flipping of surface lipoproteins through the spirochetal outer membrane.Molecular microbiology · 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
- 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
- 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
- A novel tick protein supports integrity of gut peritrophic matrix impacting existence of gut microbiome and Lyme disease pathogens.Cellular microbiology · 2021Article
- Lyme Disease Pathogenesis.Current issues in molecular biology · 2021Review
- In Silico Structural and Functional Characterization of HtrA Proteins ofTropical medicine and infectious disease · 2020Article
- Membrane directed expression in Escherichia coli of BBA57 and other virulence factors from the Lyme disease agent Borrelia burgdorferi.Scientific reports · 2019Article
- Protein Secretion in Spirochetes.Microbiology spectrum · 2019Article
- Borrelia burgdorferi protein interactions critical for microbial persistence in mammals.Cellular microbiology · 2019Review
- Assessing the Contribution of an HtrA Family Serine Protease DuringFrontiers in cellular and infection microbiology · 2019Article
- Fluorescent Proteins, Promoters, and Selectable Markers for Applications in the Lyme Disease Spirochete Borrelia burgdorferi.Applied and environmental microbiology · 2018Article
- Borrelia burgdorferi surface-located Lmp1 protein processed into region-specific polypeptides that are critical for microbial persistence.Cellular microbiology · 2018Article
- HtrA of Borrelia burgdorferi Leads to Decreased Swarm Motility and Decreased Production of Pyruvate.mBio · 2018Article
- A protein-protein interaction dictates Borrelial infectivity.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Borrelia burgdorferi gene product BB0323 is required for cell fission and pathogen persistence in vivo. Here, we show that BB0323, which is conserved among globally prevalent infectious strains, supports normal spirochaete growth and morphology even at early phases of cell division. We demonstrate that native BB0323 undergoes proteolytic processing at the C-terminus, at a site after the first 202 N-terminal amino acids. We further identified a periplasmic BB0323 binding protein in B. burgdorferi, annotated as BB0104, having serine protease activity responsible for the primary cleavage of BB0323 to produce discrete N- and C-terminal polypeptides. These two BB0323 polypeptides interact with each other, and either individually or as a complex, are associated with multiple functions in spirochaete biology and infectivity. While N-terminal BB0323 is adequate to support cell fission, the C-terminal LysM domain is dispensable for this process, despite its ability to bind B. burgdorferi peptidoglycan. However, the LysM domain or the precisely processed BB0323 product is essential for mammalian infection. As BB0323 is a membrane protein crucial for B. burgdorferi survival in vivo, exploring its function may suggest novel ways to interrupt infection while enhancing our understanding of the intricate spirochaete fission process.
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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.