ArticleJournal of bacteriology2011
Specificity and role of the Borrelia burgdorferi CtpA protease in outer membrane protein processing.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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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
21 citing papers in PubMed, 28 citations in OpenAlex.
- Complete degradation of polycyclic antibiotic methacycline by a micro/nanostructured biogenic Mn oxide composite from engineered Mn(II)-oxidizingMicrobiology spectrum · 2025Article
- Tail-specific protease is an essentialInfection and immunity · 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
- Possible effect of mutations on serological detection of Borrelia burgdorferi sensu stricto ospC major groups: An in-silico study.PloS one · 2023Article
- Bacterial Carboxyl-Terminal Processing Proteases Play Critical Roles in the Cell Envelope and Beyond.Journal of bacteriology · 2022Review
- Endogenous and Borrowed Proteolytic Activity in theMicrobiology and molecular biology reviews : MMBR · 2021Review
- The Tail-Specific Protease Is Important for Legionella pneumophila To Survive Thermal Stress in Water and inside Amoebae.Applied and environmental microbiology · 2021Article
- The C-terminus of substrates is critical but not sufficient for their degradation by theJournal of bacteriology · 2020Article
- Mutation of the Carboxy-Terminal Processing Protease inPathogens (Basel, Switzerland) · 2020Article
- Article
- Comprehensive Spatial Analysis of the Borrelia burgdorferi Lipoproteome Reveals a Compartmentalization Bias toward the Bacterial Surface.Journal of bacteriology · 2017Article
- Metabolic Adaptation of a C-Terminal Protease A-DeficientFrontiers in microbiology · 2017Article
- Lyme disease: the promise of Big Data, companion diagnostics and precision medicine.Infection and drug resistance · 2016Article
- The leptospiral outer membrane.Current topics in microbiology and immunology · 2015Review
- The lone S41 family C-terminal processing protease in Staphylococcus aureus is localized to the cell wall and contributes to virulence.Microbiology (Reading, England) · 2014Article
- Study of the protein complex, pore diameter, and pore-forming activity of the Borrelia burgdorferi P13 porin.The Journal of biological chemistry · 2014Article
- A novel carboxyl-terminal protease derived from Paenibacillus lautus CHN26 exhibiting high activities at multiple sites of substrates.BMC biotechnology · 2013Article
- The HtrA protease of Borrelia burgdorferi degrades outer membrane protein BmpD and chemotaxis phosphatase CheX.Molecular microbiology · 2013Article
- Article
- OspC is potent plasminogen receptor on surface of Borrelia burgdorferi.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
To further characterize the function of the Borrelia burgdorferi C-terminal protease CtpA, we used site-directed mutagenesis to alter the putative CtpA cleavage site of one of its known substrates, the outer membrane (OM) porin P13. These mutations resulted in only partial blockage of P13 processing. Ectopic expression of a C-terminally truncated P13 in B. burgdorferi indicated that the C-terminal peptide functions as a safeguard against misfolding or mislocalization prior to its proteolytic removal by CtpA. In a parallel study of Borrelia burgdorferi lipoprotein sorting mechanisms, we observed a lower-molecular-weight variant of surface lipoprotein OspC that was particularly prominent with OspC mutants that mislocalized to the periplasm or contained C-terminal epitope tags. Further investigation revealed that the variant resulted from C-terminal proteolysis by CtpA. Together, these findings indicate that CtpA rather promiscuously targets polypeptides that lack structurally constrained C termini, as proteolysis appears to occur independently of a specific peptide recognition sequence. Low-level processing of surface lipoproteins such as OspC suggests the presence of a CtpA-dependent quality control mechanism that may sense proper translocation of integral outer membrane proteins and surface lipoproteins by detecting the release of C-terminal peptides.
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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.