Evidence map›Paper›PMID 17239505›Full record

ArticleVaccine2007

Construction and analysis of variants of a polyvalent Lyme disease vaccine: approaches for improving the immune response to chimeric vaccinogens.

Christopher G Earnhart, Richard T Marconi

Open access · greenAbstract read
In one paragraph

Article in Vaccine, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

27 citing papers in PubMed, 45 citations in OpenAlex.

  1. Trial
  2. Review
  3. Borrelia surface proteins: new horizons in Lyme disease diagnosis.Applied microbiology and biotechnology · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Human and Veterinary Vaccines for Lyme Disease.Current issues in molecular biology · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Epitope mapping of Borrelia burgdorferi OspC protein in homodimeric fold.Protein science : a publication of the Protein Society · 2017
    Article
  20. 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

2 authors at 1 institution in 1 country.

Christopher G EarnhartDepartment of Microbiology and Immunology, Medical College of Virginia at Virginia Commonwealth University, Richmond, VA 23298-0678, USA.
Richard T Marconi
Virginia Commonwealth University Medical Center · US

Funding

Chimeric epitope based vaccines for tick borne infectionsR01AI141801 · NIAID · VIRGINIA COMMONWEALTH UNIVERSITY · PI MARCONI, RICHARD T · 2019 to 2022
$2.5M
Development of a polyvalent chimeric vaccine for Lyme diseaseR01AI067746 · NIAID · VIRGINIA COMMONWEALTH UNIVERSITY · PI MARCONI, RICHARD T · 2006 to 2010
$1.7M
NIAID NIH HHS R01 AI067746NIAID NIH HHS R01 AI141801
6 · The paper itself

Abstract

There is currently no Lyme disease vaccine commercially available for use in humans. Outer surface protein C (OspC) of the Borrelia has been widely investigated as a potential vaccinogen. At least 38 OspC types have been defined. While the antibody response to OspC is protective, the range of protection is narrow due to the localization of protective epitopes within OspC type-specific domains. To develop a broadly protective vaccine, we previously constructed a tetravalent chimeric vaccinogen containing epitopes from OspC types A, B, K, and D. While this construct elicited bactericidal antibody against strains bearing each of the four OspC types, its solubility was low, and decreasing IgG titer to epitopes near the C-terminus of the construct was observed. In this report, construct solubility and immunogenicity were increased by dialysis against an Arg/Glu buffer. We also demonstrate the immunogenicity of the construct in alum. To further optimize epitope-specific immune responses, several constructs were generated with differing epitope organization or with putative C-terminal protective motifs. Analyses of murine antibody titers and isotype profiles induced by these constructs revealed that while the C-terminal tags did not enhance antibody titer, specific epitope reorganization and reiteration did. These analyses provide important information that can be exploited in the development of chimeric vaccinogens in general.

Indexed as

Adjuvants, ImmunologicAmino Acid SequenceAnimalsAntibodies, BacterialAntigens, BacterialBacterial Outer Membrane ProteinsBase SequenceImmunoglobulin GLyme Disease VaccinesMaleMiceMice, Inbred C3HMolecular Sequence DataVaccines, SyntheticAdjuvants, ImmunologicAntibodies, BacterialAntigens, BacterialBacterial Outer Membrane ProteinsImmunoglobulin GLyme Disease VaccinesOspC proteinVaccines, Synthetic

Identifiers

PMID17239505
PMCPMC2696934
OpenAlexW2039501176

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.