ArticleMolecular microbiology2010
Translocation of Borrelia burgdorferi surface lipoprotein OspA through the outer membrane requires an unfolded conformation and can initiate at the C-terminus.
Article in Molecular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed, 41 citations in OpenAlex.
- A Borrelia burgdorferi LptD homolog is required for flipping of surface lipoproteins through the spirochetal outer membrane.Molecular microbiology · 2023Article
- Protein Secretion in Spirochetes.Microbiology spectrum · 2019Article
- Visualization of Spirochetes by Labeling Membrane Proteins With Fluorescent Biarsenical Dyes.Frontiers 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
- Some Gram-negative Lipoproteins Keep Their Surface Topology When Transplanted from One Species to Another and Deliver Foreign Polypeptides to the Bacterial Surface.Molecular & cellular proteomics : MCP · 2017Article
- Comprehensive Spatial Analysis of the Borrelia burgdorferi Lipoproteome Reveals a Compartmentalization Bias toward the Bacterial Surface.Journal of bacteriology · 2017Article
- Identification of a Large Family of Slam-Dependent Surface Lipoproteins in Gram-Negative Bacteria.Frontiers in cellular and infection microbiology · 2017Article
- Surface-Exposed Lipoproteins: An Emerging Secretion Phenomenon in Gram-Negative Bacteria.Trends in microbiology · 2016Review
- The leptospiral outer membrane.Current topics in microbiology and immunology · 2015Review
- Analyzing the molecular mechanism of lipoprotein localization in Brucella.Frontiers in microbiology · 2015Review
- Secretion of bacterial lipoproteins: through the cytoplasmic membrane, the periplasm and beyond.Biochimica et biophysica acta · 2014Review
- A call to order at the spirochaetal host-pathogen interface.Molecular microbiology · 2013Article
- A phylum level analysis reveals lipoprotein biosynthesis to be a fundamental property of bacteria.Protein & cell · 2012Review
- Probing the Borrelia burgdorferi surface lipoprotein secretion pathway using a conditionally folding protein domain.Journal of bacteriology · 2011Article
- Determination of Borrelia surface lipoprotein anchor topology by surface proteolysis.Journal of bacteriology · 2011Article
- Specificity and role of the Borrelia burgdorferi CtpA protease in outer membrane protein processing.Journal of bacteriology · 2011Article
- Surface localization determinants of Borrelia OspC/Vsp family lipoproteins.Journal of bacteriology · 2011Article
- The double life of a bacterial lipoprotein.Molecular microbiology · 2011Article
- Lipoproteins of bacterial pathogens.Infection and immunity · 2011Review
- Development and validation of a FACS-based lipoprotein localization screen in the Lyme disease spirochete Borrelia burgdorferi.BMC microbiology · 2010Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Borrelia burgdorferi surface lipoproteins are essential to the pathogenesis of Lyme borreliosis, but the mechanisms responsible for their localization are only beginning to emerge. We have previously demonstrated the critical nature of the amino-terminal 'tether' domain of the mature lipoprotein for sorting a fluorescent reporter to the Borrelia cell surface. Here, we show that individual deletion of four contiguous residues within the tether of major surface lipoprotein OspA results in its inefficient translocation across the Borrelia outer membrane. Intriguingly, C-terminal epitope tags of these N-terminal deletion mutants were selectively surface-exposed. Fold-destabilizing C-terminal point mutations and deletions did not block OspA secretion, but rather restored one of the otherwise periplasmic tether mutants to the bacterial surface. Together, these data indicate that disturbance of a confined tether feature leads to premature folding of OspA in the periplasm and thereby prevents secretion through the outer membrane. Furthermore, they suggest that OspA emerges tail-first on the bacterial surface, yet independent of a specific C-terminal targeting peptide sequence.
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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.