ArticleJournal of bacteriology2011
Probing the Borrelia burgdorferi surface lipoprotein secretion pathway using a conditionally folding protein domain.
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 13 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
13 citing papers in PubMed, 25 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
- 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
- Article
- 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
- 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
- Structural basis for complement evasion by Lyme disease pathogen Borrelia burgdorferi.The Journal of biological chemistry · 2013Article
- Determination of Borrelia surface lipoprotein anchor topology by surface proteolysis.Journal of bacteriology · 2011Article
- The surface lipoproteins of gram-negative bacteria: Protectors and foragers in harsh environments.The Journal of biological chemistryReview
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Surface lipoproteins of Borrelia spirochetes are important virulence determinants in the transmission and pathogenesis of Lyme disease and relapsing fever. To further define the conformational secretion requirements and to identify potential lipoprotein translocation intermediates associated with the bacterial outer membrane (OM), we generated constructs in which Borrelia burgdorferi outer surface lipoprotein A (OspA) was fused to calmodulin (CaM), a conserved eukaryotic protein undergoing calcium-dependent folding. Protein localization assays showed that constructs in which CaM was fused to full-length wild-type (wt) OspA or to an intact OspA N-terminal "tether" peptide retained their competence for OM translocation even in the presence of calcium. In contrast, constructs in which CaM was fused to truncated or mutant OspA N-terminal tether peptides were targeted to the periplasmic leaflet of the OM in the presence of calcium but could be flipped to the bacterial surface upon calcium chelation. This indicated that in the absence of an intact tether peptide, unfolding of the CaM moiety was required in order to facilitate OM traversal. Together, these data further support a periplasmic tether peptide-mediated mechanism to prevent premature folding of B. burgdorferi surface lipoproteins. The specific shift in the OM topology of sequence-identical lipopeptides due to a single-variable change in environmental conditions also indicates that surface-bound Borrelia lipoproteins can localize transiently to the periplasmic leaflet of the OM.
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Registered trials
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