ArticleInfection and immunity2004
Cross-species surface display of functional spirochetal lipoproteins by recombinant Borrelia burgdorferi.
Article in Infection and immunity, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
28 citing papers in PubMed, 39 citations in OpenAlex.
- A Borrelia burgdorferi LptD homolog is required for flipping of surface lipoproteins through the spirochetal outer membrane.Molecular microbiology · 2023Article
- Identification of a novel transport system in Borrelia burgdorferi that links the inner and outer membranes.Pathogens and disease · 2023Article
- Pathogenesis of Relapsing Fever.Current issues in molecular biology · 2021Review
- Lyme Disease Pathogenesis.Current issues in molecular biology · 2021Review
- The BB0345 Hypothetical Protein of Borrelia burgdorferi Is Essential for Mammalian Infection.Infection and immunity · 2020Article
- Immune Evasion Strategies of Relapsing Fever Spirochetes.Frontiers in immunology · 2020Review
- NMR metabolome of Borrelia burgdorferi in vitro and in vivo in mice.Scientific reports · 2019Article
- The RpoS Gatekeeper inFrontiers in microbiology · 2019Article
- Comprehensive Spatial Analysis of the Borrelia burgdorferi Lipoproteome Reveals a Compartmentalization Bias toward the Bacterial Surface.Journal of bacteriology · 2017Article
- Surface-Exposed Lipoproteins: An Emerging Secretion Phenomenon in Gram-Negative Bacteria.Trends in microbiology · 2016Review
- Article
- Secretion of bacterial lipoproteins: through the cytoplasmic membrane, the periplasm and beyond.Biochimica et biophysica acta · 2014Review
- Fibronectin-binding protein of Borrelia hermsii expressed in the blood of mice with relapsing fever.Infection and immunity · 2014Article
- Article
- Contribution of the infection-associated complement regulator-acquiring surface protein 4 (ErpC) to complement resistance of Borrelia burgdorferi.Clinical & developmental immunology · 2012Article
- 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
- Surface localization determinants of Borrelia OspC/Vsp family lipoproteins.Journal of bacteriology · 2011Article
- Interaction of variable bacterial outer membrane lipoproteins with brain endothelium.PloS one · 2010Article
- Translocation of Borrelia burgdorferi surface lipoprotein OspA through the outer membrane requires an unfolded conformation and can initiate at the C-terminus.Molecular microbiology · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 4 institutions in 1 country.
Funding
Abstract
Surface-exposed lipoproteins of relapsing fever (RF) and Lyme borreliosis Borrelia spirochetes mediate certain interactions of the bacteria with their arthropod and vertebrate hosts. RF spirochetes such as Borrelia hermsii serially evade the host's antibody response by multiphasic antigenic variation of Vsp and Vlp proteins. Furthermore, the expression of Vsp1 and Vsp2 by Borrelia turicatae is associated with neurotropism and higher blood densities, respectively. In contrast to RF Borrelia species, the Lyme borreliosis spirochete Borrelia burgdorferi is amenable to genetic manipulation. To facilitate structure-function analyses of RF surface lipoproteins, we used recombinant plasmids to introduce full-length vsp1 and vsp2 as well as two representative vlp genes into B. burgdorferi cells. Recombinant B. burgdorferi cells constitutively expressed the proteins under the control of the B. burgdorferi flaB promoter. Antibody and protease accessibility assays indicated proper surface exposure and folding. Expression of Vsp1 and Vsp2 conferred glycosaminoglycan binding to recombinant B. burgdorferi cells that was similar to that observed with purified recombinant proteins and B. turicatae expressing native Vsp. These data demonstrate that the lipoprotein modification and export mechanisms in the genus Borrelia are conserved. They also validate the use of recombinant B. burgdorferi in studies of surface lipoprotein structure-function and the biogenesis of spirochete membranes.
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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.