Evidence map›Paper›PMID 22083700›Full record

ArticleInfection and immunity2012

The enolase of Borrelia burgdorferi is a plasminogen receptor released in outer membrane vesicles.

A Toledo, J L Coleman, C J Kuhlow, J T Crowley, J L Benach

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 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

64 citing papers in PubMed, 102 citations in OpenAlex.

  1. Surface enolase is a virulence factor ofFrontiers in microbiology · 2026
    Article
  2. Review
  3. Article
  4. Evaluating Outer Membrane Vesicle Isolation Techniques forAntibiotics (Basel, Switzerland) · 2025
    Article
  5. Functional Cargo in Membrane Vesicles From a Citrus Pathogen.Environmental microbiology reports · 2025
    Article
  6. 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
  7. Review
  8. Article
  9. Purification of Borrelia burgdorferi Outer Membrane Vesicles.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Microorganisms · 2022
    Article
  15. Streptomyces coelicolor Vesicles: Many Molecules To Be Delivered.Applied and environmental microbiology · 2022
    Article
  16. Review
  17. Review
  18. Review
  19. Endogenous and Borrowed Proteolytic Activity in theMicrobiology and molecular biology reviews : MMBR · 2021
    Review
  20. Article

4 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

A ToledoDepartment of Molecular Genetics and Microbiology, Center for Infectious Diseases, Stony Brook University, Stony Brook, New York, USA.
J L Coleman
C J Kuhlow
J T Crowley
J L Benach
Stony Brook University · US

Funding

BORRELIA BURGDORFERI--INVASION AND CHRONICITYR01AR040445 · NIAMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI BENACH, JORGE L. · 1990 to 2011
$4.1M
Antigen Specific Response to BorreliaR01AI027044 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI BENACH, JORGE L. · 1989 to 2020
$3.7M
NIAID NIH HHS R01 AI027044NIAID NIH HHS R01-AI-027044NIAID NIH HHS U54-AI-0715558NIAMS NIH HHS R01 AR040445NIAMS NIH HHS R01-AR-040445
6 · The paper itself

Abstract

The agent of Lyme disease, Borrelia burgdorferi, has a number of outer membrane proteins that are differentially regulated during its life cycle. In addition to their physiological functions in the organism, these proteins also likely serve different functions in invasiveness and immune evasion. In borreliae, as well as in other bacteria, a number of membrane proteins have been implicated in binding plasminogen. The activation and transformation of plasminogen into its proteolytically active form, plasmin, enhances the ability of the bacteria to disseminate in the host. Outer membrane vesicles of B. burgdorferi contain enolase, a glycolytic-cycle enzyme that catalyzes 2-phosphoglycerate to form phosphoenolpyruvate, which is also a known plasminogen receptor in Gram-positive bacteria. The enolase was cloned, expressed, purified, and used to generate rabbit antienolase serum. The enolase binds plasminogen in a lysine-dependent manner but not through ionic interactions. Although it is present in the outer membrane, microscopy and proteinase K treatment showed that enolase does not appear to be exposed on the surface. However, enolase in the outer membrane vesicles is accessible to proteolytic degradation by proteinase K. Samples from experimentally and tick-infected mice and rabbits as well as from Lyme disease patients exhibit recognition of enolase in serologic assays. Thus, this immunogenic plasminogen receptor released in outer membrane vesicles could be responsible for external proteolysis in the pericellular environment and have roles in nutrition and in enhancing dissemination.

Indexed as

AnimalsAntibodies, BacterialBorrelia burgdorferiCloning, MolecularExosomesFemaleHumansMiceMice, Inbred C3HPhosphopyruvate HydratasePlasminogenProtein BindingProtein Interaction MappingRabbitsRecombinant ProteinsVirulence FactorsAntibodies, BacterialPhosphopyruvate HydratasePlasminogenRecombinant ProteinsVirulence Factors

Identifiers

PMID22083700
PMCPMC3255694
OpenAlexW2150922454

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.