Evidence map›Paper›PMID 7790053›Full record

ArticleInfection and immunity1995

Membrane topology of Borrelia burgdorferi and Treponema pallidum lipoproteins.

J D Jones, K W Bourell, M V Norgard, J D Radolf

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

30 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
  2. Review
  3. Lyme Disease in Humans.Current issues in molecular biology · 2021
    Article
  4. Review
  5. Hypercholesterolemia and ApoE deficiency result in severe infection with Lyme disease and relapsing-fever Borrelia.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
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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

4 authors at 1 institution in 1 country.

J D JonesDepartment of Microbiology, University of Texas, Southwestern Medical Center at Dallas 75235, USA.
K W Bourell
M V Norgard
J D Radolf
The University of Texas Southwestern Medical Center · US

Funding

RpoS Regulation of Borrelia burgdorferi Genes in vivoR01AI029735 · NIAID · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI CAIMANO, MELISSA J, RADOLF, JUSTIN D · 1990 to 2022
$10.7M
Treponema pallidum Outer Membrane Proteins and Transition Metal AcquisitionR01AI026756 · NIAID · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI RADOLF, JUSTIN D · 1992 to 2017
$5.1M
MOLECULAR ANALYSIS OF T PALLIDUM MEMBRANE PROTEINSR01AI016692 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI NORGARD, MICHAEL V. · 1986 to 2009
$4.6M
T.pallidum Membrane Immunogens and Anti-Oxidant DefenseR37AI026756 · NIAID · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI RADOLF, JUSTIN D · 2002 to 2006
$1.8M
MEMBRANE PROTEINS OF TREPONEMA PALLIDUMR29AI026756 · NIAID · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI RADOLF, JUSTIN D. · 1988 to 1991
–
NIAID NIH HHS AI-16692NIAID NIH HHS AI26756NIAID NIH HHS AI-29735
6 · The paper itself

Abstract

A critical issue regarding the molecular architectures of Treponema pallidum and Borrelia burgdorferi, the agents of venereal syphilis and Lyme disease, respectively, concerns the membrane topologies of their major lipoprotein immunogens. A related question is whether these lipid-modified membrane proteins form intramembranous particles during freeze fracture electron microscopy. To address these issues, native borrelial and treponemal lipoproteins were reconstituted into liposomes of diverse composition. The importance of the covalently associated lipids for membrane association of lipoproteins was revealed by the observation that nonlipidated recombinant forms of both B. burgdorferi OspA and the T. pallidum 47-kDa immunogen (Tpp47) showed very weak or no binding to model bilayer vesicles. In contrast to control liposomes reconstituted with bacteriorhodopsin or bovine rhodopsin, two well-characterized transmembrane proteins, none of the lipoprotein-liposomes contained particles when examined by freeze fracture electron microscopy. To extend these findings to prokaryotic lipoproteins with relatively amphiphilic polypeptides, similar experiments were conducted with a recombinant nonlipidated form of Escherichia coli TraT, a lipoprotein which has putative transmembrane domains. The nonlipidated TraT oligomers bound vesicles derived from E. coli lipids but, surprisingly, did not form particles in the freeze-fractured liposomes. These findings support (i) a proposed topology of spirochetal lipoproteins in which the polypeptide is extrinsic to the membrane surface and (ii) the contention that particles visualized in freeze-fractured spirochetal membranes represent poorly characterized transmembrane proteins.

Indexed as

Antigens, SurfaceBacterial Outer Membrane ProteinsBacterial VaccinesBacteriorhodopsinsBase SequenceBorrelia burgdorferi GroupCell MembraneFreeze FracturingLipid BilayersLipoproteinsLiposomesMolecular Sequence DataOligonucleotide ProbesRecombinant ProteinsTreponema pallidumAntigens, SurfaceBacterial Outer Membrane ProteinsBacterial VaccinesBacteriorhodopsinsLipid BilayersLipoproteinsLiposomesOligonucleotide ProbesOspA proteinRecombinant Proteins

Identifiers

PMID7790053
PMCPMC173324
OpenAlexW2224089154

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.