Evidence map›Paper›PMID 22025510›Full record

ArticleInfection and immunity2012

A surface enolase participates in Borrelia burgdorferi-plasminogen interaction and contributes to pathogen survival within feeding ticks.

Sarah Veloso Nogueira, Alexis A Smith, Jin-Hong Qin, Utpal Pal

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

41 citing papers in PubMed, 66 citations in OpenAlex.

  1. Trial
  2. Characterization ofMicroorganisms · 2026
    Article
  3. The Regulatory Mechanisms of Treponema pallidum Enolase on Macrophages: From Enzymatic Activity to Signal Transduction.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Endogenous and Borrowed Proteolytic Activity in theMicrobiology and molecular biology reviews : MMBR · 2021
    Review
  9. Article
  10. Pathogens (Basel, Switzerland) · 2021
    Article
  11. Interactions Between Ticks and Lyme Disease Spirochetes.Current issues in molecular biology · 2021
    Article
  12. PreventingEmerging microbes & infections · 2020
    Article
  13. Article
  14. Article
  15. Protein Secretion in Spirochetes.Microbiology spectrum · 2019
    Article
  16. Review
  17. Enolase FromFrontiers in immunology · 2019
    Article
  18. Article
  19. 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

4 authors at 2 institutions in 1 country.

Sarah Veloso NogueiraDepartment of Veterinary Medicine, University of Maryland, College Park, Maryland 20742, USA.
Alexis A Smith
Jin-Hong Qin
Utpal Pal
Virginia–Maryland College of Veterinary Medicine · USUniversity of Maryland, College Park · US

Funding

BORRELIA GENE PRODUCTS CRITICAL FOR NATURAL INFECTION CYCLER01AI080615 · NIAID · UNIV OF MARYLAND, COLLEGE PARK · PI PAL, UTPAL · 2009 to 2024
$5.2M
Borella Gene Products Critical For Natural Infection CycleR56AI080615 · NIAID · UNIV OF MARYLAND, COLLEGE PARK · PI PAL, UTPAL · 2013 to 2013
$357k
NIAID NIH HHS R01 AI080615NIAID NIH HHS R56 AI080615
6 · The paper itself

Abstract

Borrelia burgdorferi, a tick-borne bacterial pathogen, causes a disseminated infection involving multiple organs known as Lyme disease. Surface proteins can directly participate in microbial virulence by facilitating pathogen dissemination via interaction with host factors. We show here that a fraction of the B. burgdorferi chromosomal gene product BB0337, annotated as enolase or phosphopyruvate dehydratase, is associated with spirochete outer membrane and is surface exposed. B. burgdorferi enolase, either in a recombinant form or as a membrane-bound native antigen, displays enzymatic activities intrinsic to the glycolytic pathway. However, the protein also interacts with host plasminogen, potentially leading to its activation and resulting in B. burgdorferi-induced fibrinolysis. As expected, enolase displayed consistent expression in vivo, however, with a variable temporal and spatial expression during spirochete infection in mice and ticks. Despite an extracellular exposure of the antigen and a potential role in host-pathogen interaction, active immunization of mice with recombinant enolase failed to evoke protective immunity against subsequent B. burgdorferi infection. In contrast, enolase immunization of murine hosts significantly reduced the acquisition of spirochetes by feeding ticks, suggesting that the protein could have a stage-specific role in B. burgdorferi survival in the feeding vector. Strategies to interfere with the function of surface enolase could contribute to the development of novel preventive measures to interrupt the spirochete infection cycle and reduce the incidences of Lyme disease.

Indexed as

Host-Pathogen InteractionsMicrobial ViabilityAnimalsBacterial Outer Membrane ProteinsBacterial ProteinsBorrelia burgdorferiFemaleFibrinolysisGene Expression ProfilingMiceMice, Inbred C3HPhosphopyruvate HydratasePlasminogenProtein BindingProtein Interaction MappingTicksBacterial Outer Membrane ProteinsBacterial ProteinsPhosphopyruvate HydratasePlasminogen

Identifiers

PMID22025510
PMCPMC3255677
OpenAlexW2167387211

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.