Evidence map›Paper›PMID 37170643›Full record

ArticleMolecular microbiology2023

A Borrelia burgdorferi LptD homolog is required for flipping of surface lipoproteins through the spirochetal outer membrane.

Huan He, Ankita S Pramanik, Selene K Swanson, David K Johnson, Laurence Florens, Wolfram R Zückert

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
5.6field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Identification and characterization of the functional LolB ortholog inbioRxiv : the preprint server for biology · 2026
    Article
  6. Small siphophage binding to an open state of the LptDE outer membrane lipopolysaccharide translocon.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Identification and characterization of the lipoproteinProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Review
  15. Article
  16. bioRxiv : the preprint server for biology · 2024
    Article
  17. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Huan HeDepartment of Microbiology, Molecular Genetics and Immunology, University of Kansas School of Medicine, Kansas City, Kansas, USA.
Ankita S PramanikDepartment of Microbiology, Molecular Genetics and Immunology, University of Kansas School of Medicine, Kansas City, Kansas, USA.
Selene K SwansonStowers Institute for Medical Research, Kansas City, Missouri, USA.
David K JohnsonComputational Chemical Biology Core, University of Kansas, Lawrence, Kansas, USA.
Laurence FlorensStowers Institute for Medical Research, Kansas City, Missouri, USA.
Wolfram R ZückertDepartment of Microbiology, Molecular Genetics and Immunology, University of Kansas School of Medicine, Kansas City, Kansas, USA.ORCID 0000-0002-7350-2162
University of Kansas · USStowers Institute for Medical Research · US

Funding

Synthetic Chemical Biology CoreP20GM113117 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI OROZCO, ROBIN C. · 2016 to 2025
$23.9M
Role of Borrelia Lpt Homologs in Surface Lipoprotein SecretionR21AI173835 · NIAID · UNIVERSITY OF KANSAS MEDICAL CENTER · PI ZUECKERT, WOLFRAM R · 2023 to 2024
$426k
Chaperone-Mediated Secretion of Borrelia LipoproteinsR21AI144624 · NIAID · UNIVERSITY OF KANSAS MEDICAL CENTER · PI ZUECKERT, WOLFRAM R · 2019 to 2020
$413k
NIAID NIH HHS R21 AI144624NIAID NIH HHS R21 AI173835NIGMS NIH HHS P20 GM113117NIH HHS P20 GM113117
6 · The paper itself

Abstract

Borrelia spirochetes are unique among diderm bacteria in their lack of lipopolysaccharide (LPS) in the outer membrane (OM) and their abundance of surface-exposed lipoproteins with major roles in transmission, virulence, and pathogenesis. Despite their importance, little is known about how surface lipoproteins are translocated through the periplasm and the OM. Here, we characterized Borrelia burgdorferi BB0838, a distant homolog of the OM LPS assembly protein LptD. Using a CRISPR interference approach, we showed that BB0838 is required for cell growth and envelope stability. Upon BB0838 knockdown, surface lipoprotein OspA was retained in the inner leaflet of the OM, as determined by its inaccessibility to in situ proteolysis but its presence in OM vesicles. The topology of the OM porin/adhesin P66 remained unaffected. Quantitative mass spectrometry of the B. burgdorferi membrane-associated proteome confirmed the selective periplasmic retention of surface lipoproteins under BB0838 knockdown conditions. Additional analysis identified a single in situ protease-accessible BB0838 peptide that mapped to a predicted β-barrel surface loop. Alphafold Multimer modeled a B. burgdorferi LptB

Indexed as

Borrelia burgdorferiBacteriaBacterial Outer Membrane ProteinsLipopolysaccharidesLipoproteinsBacterial Outer Membrane ProteinsLipopolysaccharidesLipoproteinsCRISPRienvelope biogenesislipoproteinmembrane proteinprotein secretionspirochete

Identifiers

PMID37170643
PMCPMC10330739
OpenAlexW4376224871

What OpenQuestion holds

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Registered trials

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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.