ArticleJournal of bacteriology2011
Surface localization determinants of Borrelia OspC/Vsp family lipoproteins.
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 22 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 40 citations in OpenAlex.
- Outer membrane lipoproteins: late to the party, but the center of attention.Journal of bacteriology · 2025Review
- Article
- A Borrelia burgdorferi LptD homolog is required for flipping of surface lipoproteins through the spirochetal outer membrane.Molecular microbiology · 2023Article
- Article
- Protein Secretion in Spirochetes.Microbiology spectrum · 2019Article
- Lipoproteins and Their Trafficking to the Outer Membrane.EcoSal Plus · 2019Review
- Comprehensive Spatial Analysis of the Borrelia burgdorferi Lipoproteome Reveals a Compartmentalization Bias toward the Bacterial Surface.Journal of bacteriology · 2017Article
- Article
- Surface-Exposed Lipoproteins: An Emerging Secretion Phenomenon in Gram-Negative Bacteria.Trends in microbiology · 2016Review
- Analyzing the molecular mechanism of lipoprotein localization in Brucella.Frontiers in microbiology · 2015Review
- The leptospiral outer membrane.Current topics in microbiology and immunology · 2015Review
- Transmembrane domain of surface-exposed outer membrane lipoprotein RcsF is threaded through the lumen of β-barrel proteins.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Secretion of bacterial lipoproteins: through the cytoplasmic membrane, the periplasm and beyond.Biochimica et biophysica acta · 2014Review
- Deciphering protein stability in cells.Journal of molecular biology · 2014Article
- Distribution of cp32 prophages among Lyme disease-causing spirochetes and natural diversity of their lipoprotein-encoding erp loci.Applied and environmental microbiology · 2013Article
- A call to order at the spirochaetal host-pathogen interface.Molecular microbiology · 2013Article
- Phosphatidylglycerol::prolipoprotein diacylglyceryl transferase (Lgt) of Escherichia coli has seven transmembrane segments, and its essential residues are embedded in the membrane.Journal of bacteriology · 2012Article
- 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
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The dimeric OspC/Vsp family surface lipoproteins of Borrelia spirochetes are crucial to the transmission and persistence of Lyme borreliosis and tick-borne relapsing fever. However, the requirements for their proper surface display remained undefined. In previous studies, we showed that localization of Borrelia burgdorferi monomeric surface lipoprotein OspA was dependent on residues in the N-terminal "tether" peptide. Here, site-directed mutagenesis of the B. burgdorferi OspC tether revealed two distinct regions affecting either release from the inner membrane or translocation through the outer membrane. Determinants of both of these steps appear consolidated within a single region of the Borrelia turicatae Vsp1 tether. Periplasmic OspC mutants still were able to form dimers. Their localization defect could be rescued by the addition of an apparently structure-destabilizing C-terminal epitope tag but not by coexpression with wild-type OspC. Furthermore, disruption of intermolecular Vsp1 salt bridges blocked dimerization but not surface localization of the resulting Vsp1 monomers. Together, these results suggest that Borrelia OspC/Vsp1 surface lipoproteins traverse the periplasm and the outer membrane as unfolded monomeric intermediates and assemble into their functional multimeric folds only upon reaching the spirochetal surface.
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What OpenQuestion holds
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.