Evidence map›Paper›PMID 16740958›Full record

ArticleJournal of bacteriology2006

Crystal structure of neurotropism-associated variable surface protein 1 (Vsp1) of Borrelia turicatae.

Catherine L Lawson, Brian H Yung, Alan G Barbour, Wolfram R Zückert

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.2field-weighted citation impact, top 48% 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

19 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Pathogenesis of Relapsing Fever.Current issues in molecular biology · 2021
    Review
  6. Review
  7. Relapsing Fevers: Neglected Tick-Borne Diseases.Frontiers in cellular and infection microbiology · 2018
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
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 3 institutions in 1 country.

Catherine L LawsonDepartment of Chemistry and Chemical Biology, 610 Taylor Road, Piscataway, NJ 08854, USA. cathy.lawson@rutgers.edu
Brian H Yung
Alan G Barbour
Wolfram R Zückert
Rutgers, The State University of New Jersey · USUniversity of California, Irvine · USUniversity of Kansas Medical Center · US

Funding

MOLECULAR BASIS OF BORRELIA PATHOGENESISR37AI024424 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI BARBOUR, ALAN G. · 2001 to 2010
$3.5M
VACCINE INTERVENTION FOR LYME BORRELIOSISR01AI037256 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI DUNN, JOHN J · 1994 to 2002
$1.7M
MOLECULAR BASIS OF BORRELIA PATHOGENESISR01AI024424 · NIAID · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI BARBOUR, ALAN G. · 1987 to 2000
$339k
Structure-Function of Borrelia Surface LipoproteinsR03AI059468 · NIAID · UNIVERSITY OF KANSAS MEDICAL CENTER · PI ZUECKERT, WOLFRAM R · 2004 to 2005
$147k
NIAID NIH HHS AI24424NIAID NIH HHS AI37256NIAID NIH HHS AI59468NIAID NIH HHS R01 AI024424NIAID NIH HHS R03 AI059468NIAID NIH HHS R37 AI024424
6 · The paper itself

Abstract

Vsp surface lipoproteins are serotype-defining antigens of relapsing fever spirochetes that undergo multiphasic antigenic variation to allow bacterial persistence in spite of an immune response. Two isogenic serotypes of Borrelia turicatae strain Oz1 differ in their Vsp sequences and in disease manifestations in infected mice: Vsp1 is associated with the selection of a neurological niche, while Vsp2 is associated with blood and skin infection. We report here crystal structures of the Vsp1 dimer at 2.7 and 2.2 A. The structures confirm that relapsing fever Vsp proteins share a common helical fold with OspCs of Lyme disease-causing Borrelia. The fold features an inner stem formed by highly conserved N and C termini and an outer "dome" formed by the variable central residues. Both Vsp1 and OspC structures possess small water-filled cavities, or pockets, that are lined largely by variable residues and are thus highly variable in shape. These features appear to signify tolerance of the Vsp-OspC fold for imperfect packing of residues at its antigenic surface. Structural comparison of Vsp1 with a homology model for Vsp2 suggests that observed differences in disease manifestation may arise in part from distinct differences in electrostatic surface properties; additional predicted positively charged surface patches on Vsp2 compared to Vsp1 may be sufficient to explain the relative propensity of Vsp2 to bind to acidic glycosaminoglycans.

Indexed as

Antigens, BacterialBacterial Outer Membrane ProteinsBorreliaCrystallizationDimerizationEscherichia coliLipoproteinsMembrane ProteinsModels, MolecularMolecular Sequence DataProtein FoldingRecombinant ProteinsRelapsing FeverStatic ElectricityAntigens, BacterialBacterial Outer Membrane ProteinsLipoproteinsMembrane ProteinsOspC proteinRecombinant Proteins

Identifiers

PMID16740958
PMCPMC1482977
OpenAlexW2114455781

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.