Evidence map›Paper›PMID 22128161›Full record

ArticleThe Journal of biological chemistry2012

Novel mycobacteria antigen 85 complex binding motif on fibronectin.

Chih-Jung Kuo, Hannah Bell, Ching-Lin Hsieh, Christopher P Ptak, Yung-Fu Chang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

30 citing papers in PubMed, 53 citations in OpenAlex.

  1. Antigen 85B ofVaccines · 2026
    Review
  2. Article
  3. Article
  4. Circulating antibody signatures againstFrontiers in immunology · 2026
    Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Bioprospective Role ofMolecules (Basel, Switzerland) · 2023
    Review
  11. Nano-Delivery System of Ethanolic Extract of Propolis TargetingNanomaterials (Basel, Switzerland) · 2023
    Article
  12. Review
  13. Article
  14. Review
  15. Immunomodulatory Effects of RecombinantPathogens (Basel, Switzerland) · 2020
    Article
  16. Review
  17. Article
  18. Article
  19. Frontiers in cellular and infection microbiology · 2017
    Article
  20. Pathogenesis, Molecular Genetics, and Genomics ofFrontiers in veterinary science · 2017
    Review
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.

Chih-Jung KuoDepartment of Population Medicine and Diagnostic Sciences, College of Veterinary Medicine, Cornell University, Ithaca, New York 14853, USA.
Hannah Bell
Ching-Lin Hsieh
Christopher P Ptak
Yung-Fu Chang
Cornell University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The members of the antigen 85 protein family (Ag85), consisting of members Ag85A, Ag85B, and Ag85C, are the predominantly secreted proteins of mycobacteria and possess the ability to specifically interact with fibronectin (Fn). Because Fn-binding proteins are likely to be important virulence factors of Mycobacterium spp., Ag85 may contribute to the adherence, invasion, and dissemination of organisms in host tissue. In this study, we reported the Fn binding affinity of Ag85A, Ag85B, and Ag85C from Mycobacterium avium subsp. paratuberculosis (MAP) (K(D) values were determined from 33.6 to 68.4 nm) and mapped the Ag85-binding motifs of Fn. Fn14, a type III module located on the heparin-binding domain II (Hep-2) of Fn, was discovered to interact with Ag85 from MAP. The peptide inhibition assay subsequently demonstrated that a peptide consisting of residues 17-26 from Fn14 ((17)SLLVSWQPPR(26), termed P17-26) could interfere with Ag85B binding to Fn (73.3% reduction). In addition, single alanine substitutions along the sequence of P17-26 revealed that the key residues involved in Ag85-Fn binding likely contribute through hydrophobic and charge interactions. Moreover, binding of Ag85 on Fn siRNA-transfected Caco2 cells was dramatically reduced (44.6%), implying the physiological significance of the Ag85-Fn interaction between mycobacteria and host cells during infection. Our results indicate that Ag85 binds to Fn at a novel motif and plays a critical role in mycobacteria adherence to host cells by initiating infection. Ag85 might serve as an important colonization factor potentially contributing to mycobacterial virulence.

Indexed as

Amino Acid MotifsAntigens, BacterialCaco-2 CellsFibronectinsHost-Pathogen InteractionsHumansHydrophobic and Hydrophilic InteractionsMycobacterium aviumMycobacterium avium subsp. paratuberculosisParatuberculosisProtein BindingProtein Structure, TertiaryAntigens, BacterialFibronectins

Identifiers

PMID22128161
PMCPMC3265870
OpenAlexW2140233090

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.