Evidence map›Paper›PMID 22801575›Full record

ArticleImmunology and cell biology2012

HspX-mediated protection against tuberculosis depends on its chaperoning of a mycobacterial molecule.

Jennifer L Taylor, Agatha Wieczorek, Andrew R Keyser, Ajay Grover, Rachel Flinkstrom, Russell K Karls, Helle Bielefeldt-Ohmann, Karen M Dobos, Angelo A Izzo

Open access · hybridAbstract read
In one paragraph

Article in Immunology and cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

26 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Recent Characterization of Key Proteins to Combat Tuberculosis.Advances in experimental medicine and biology · 2026
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Liposomal delivery system/adjuvant for tuberculosis vaccine.Immunity, inflammation and disease · 2023
    Review
  10. Review
  11. Review
  12. Article
  13. AFrontiers in immunology · 2021
    Article
  14. Comparison of hspX gene sequence in the Beijing and non-BeijingJournal of clinical tuberculosis and other mycobacterial diseases · 2020
    Article
  15. Article
  16. Article
  17. Article
  18. Design and Construction of a Cloning Vector Containing theReports of biochemistry & molecular biology · 2016
    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

9 authors at 3 institutions in 2 countries.

Jennifer L TaylorDepartment of Microbiology, Mycobacteria Research Laboratories, Immunology and Pathology, Colorado State University, Fort Collins, CO 80523-1682, USA. Jennifer.L.Taylor@Colostate.edu
Agatha Wieczorek
Andrew R Keyser
Ajay Grover
Rachel Flinkstrom
Russell K Karls
Helle Bielefeldt-Ohmann
Karen M Dobos
Angelo A Izzo
Colorado State University · USUniversity of Georgia · USUniversity of Queensland · AU

Funding

NIAID NIH HHS N01 AI040091
6 · The paper itself

Abstract

New approaches consisting of 'multistage' vaccines against (TB) are emerging that combine early antigenic proteins with latency-associated antigens. In this study, HspX was tested for its potential to elicit both short- and long-term protective immune responses. HspX is a logical component in vaccine strategies targeting protective immune responses against primary infection, as well as against reactivation of latent infection, because as previously shown, it is produced during latency, and as our studies show, it elicits protection within 30 days of infection. Recent studies have shown that the current TB vaccine, bacilli Calmette-Guerin (BCG), does not induce strong interferon-γ T-cell responses to latency-associated antigens like HspX, which may be in part why BCG fails to protect against reactivation disease. We therefore tested HspX protein alone as a prophylactic vaccine and as a boost to BCG vaccination, and found that HspX purified from M. tuberculosis cell lysates protected mice against aerosol challenge and improved the protective efficacy of BCG when used as a booster vaccine. Native HspX was highly immunogenic and protective, in a dose-dependent manner, in both short- and long-term infection models. Based on these promising findings, HspX was produced as a recombinant protein in E. coli, as this would enable facile purification; however, recombinant HspX (rHspX) alone consistently failed to protect against aerosol challenge. Incubation of rHspX with mycobacterial cell lysate and re-purification following incubation restored the capacity of the protein to confer protection. These data suggest the possibility that the native form may chaperone an immunogenic and protective antigen that is mycobacteria-specific.

Indexed as

AnimalsAntigens, BacterialBacterial ProteinsCells, CulturedEscherichia coliFemaleHumansImmunity, ActiveInterferon-gammaMiceMice, Inbred C57BLMolecular ChaperonesTransgenesTuberculosisTuberculosis VaccinesAntigens, BacterialBacterial ProteinsHspX protein, Mycobacterium tuberculosisInterferon-gammaMolecular ChaperonesTuberculosis Vaccines

Identifiers

PMID22801575
PMCPMC3511932
OpenAlexW1980858914

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.