Evidence map›Paper›PMID 25332123›Full record

ArticleInfection and immunity2015

CFP-10 from Mycobacterium tuberculosis selectively activates human neutrophils through a pertussis toxin-sensitive chemotactic receptor.

Amanda Welin, Halla Björnsdottir, Malene Winther, Karin Christenson, Tudor Oprea, Anna Karlsson, Huamei Forsman, Claes Dahlgren, Johan Bylund

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed, 1 pooled it
1.3field-weighted citation impact, top 21% 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

22 citing papers in PubMed, 1 synthesis or guideline pooled it, 43 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Circulating antibody signatures againstFrontiers in immunology · 2026
    Article
  5. Protein-Mediated Virulence in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026
    Review
  6. Article
  7. Quantum Dot-Based Nanosensors for In Vitro Detection ofNanomaterials (Basel, Switzerland) · 2024
    Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Role of phagocyte extracellular traps duringFrontiers in microbiology · 2023
    Review
  13. Article
  14. A scientometrics study of the nanomedicines assisted in respiratory diseases.Frontiers in bioengineering and biotechnology · 2022
    Article
  15. Review
  16. Review
  17. Frontiers in cellular and infection microbiology · 2020
    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

9 authors at 2 institutions in 2 countries.

Amanda WelinThe Phagocyte Research Group, Department of Rheumatology and Inflammation Research, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden amanda.welin@gu.se.
Halla BjörnsdottirThe Phagocyte Research Group, Department of Rheumatology and Inflammation Research, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden.
Malene WintherThe Phagocyte Research Group, Department of Rheumatology and Inflammation Research, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden.
Karin ChristensonThe Phagocyte Research Group, Department of Rheumatology and Inflammation Research, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden.
Tudor OpreaThe Phagocyte Research Group, Department of Rheumatology and Inflammation Research, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden Division of Biocomputing, Department of Molecular Biology, University of New Mexico Health Sciences Center, Albuquerque, New Mexico, USA.
Anna KarlssonThe Phagocyte Research Group, Department of Rheumatology and Inflammation Research, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden.
Huamei ForsmanThe Phagocyte Research Group, Department of Rheumatology and Inflammation Research, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden.
Claes DahlgrenThe Phagocyte Research Group, Department of Rheumatology and Inflammation Research, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden.
Johan BylundThe Phagocyte Research Group, Department of Rheumatology and Inflammation Research, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden Department of Oral Microbiology and Immunology, Sahlgrenska Academy at University of Gothenburg, Gothenburg, Sweden.
University of Gothenburg · SEUniversity of New Mexico · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Upon infection with Mycobacterium tuberculosis, neutrophils are massively recruited to the lungs, but the role of these cells in combating the infection is poorly understood. Through a type VII secretion system, M. tuberculosis releases a heterodimeric protein complex, containing a 6-kDa early secreted antigenic target (ESAT-6) and a 10-kDa culture filtrate protein (CFP-10), that is essential for virulence. Whereas the ESAT-6 component possesses multiple virulence-related activities, no direct biological activity of CFP-10 has been shown, and CFP-10 has been described as a chaperone protein for ESAT-6. We here show that the ESAT-6:CFP-10 complex induces a transient release of Ca(2+) from intracellular stores in human neutrophils. Surprisingly, CFP-10 rather than ESAT-6 was responsible for triggering the Ca(2+) response, in a pertussis toxin-sensitive manner, suggesting the involvement of a G-protein-coupled receptor. In line with this, the response was accompanied by neutrophil chemotaxis and activation of the superoxide-producing NADPH-oxidase. Neutrophils were unique among leukocytes in responding to CFP-10, as monocytes and lymphocytes failed to produce a Ca(2+) signal upon stimulation with the M. tuberculosis protein. Hence, CFP-10 may contribute specifically to neutrophil recruitment and activation during M. tuberculosis infection, representing a novel biological role for CFP-10 in the ESAT-6:CFP-10 complex, beyond the previously described chaperone function.

Indexed as

Antigens, BacterialBacterial ProteinsCalciumCells, CulturedChemotaxisHumansMycobacterium tuberculosisNADPH OxidasesNeutrophilsAntigens, BacterialBacterial ProteinsCalciumCFP-10 protein, Mycobacterium tuberculosisESAT-6 protein, Mycobacterium tuberculosisNADPH Oxidases

Identifiers

PMID25332123
PMCPMC4288871
OpenAlexW2117745740

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.