Evidence map›Paper›PMID 9770536›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

Molecular characterization of the mycobacterial heparin-binding hemagglutinin, a mycobacterial adhesin.

F D Menozzi, R Bischoff, E Fort, M J Brennan, C Locht

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

68 citing papers in PubMed, 156 citations in OpenAlex.

  1. Article
  2. In silico design ofHeliyon · 2024
    Article
  3. Article
  4. Article
  5. Review
  6. New Insights into the Methylation ofPathogens (Basel, Switzerland) · 2021
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. The Heparin-Binding Hemagglutinin ofFrontiers in cellular and infection microbiology · 2020
    Article
  12. Adhesion molecules facilitate host-pathogen interaction & mediateThe Indian journal of medical research · 2019
    Review
  13. Lectins ofBeilstein journal of organic chemistry · 2019
    Review
  14. Article
  15. Article
  16. Glycobiology of syndecan-1 in bacterial infections.Biochemical Society transactions · 2018
    Review
  17. Review
  18. Immunogenicity of heparin-binding hemagglutinin expressed byIranian journal of basic medical sciences · 2018
    Article
  19. Article
  20. Frontiers in cellular and infection microbiology · 2018
    Review

8 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 4 institutions in 2 countries.

F D MenozziLaboratoire de Microbiologie Génétique et Moléculaire, Institut National de la Santé et de la Recherche Médicale U447, Institut Pasteur de Lille, 1 rue Calmette, F-59019 Lille Cedex, France.
R Bischoff
E Fort
M J Brennan
C Locht
Inserm · FRCenter for Biologics Evaluation and Research · USInstitut de Biologie de Lille · FRTransgene (France) · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although it generally is accepted that the interaction of Mycobacterium tuberculosis with alveolar macrophages is a key step in the pathogenesis of tuberculosis, interactions with other cell types, especially epithelial cells, also may be important. In this study we describe the molecular characterization of a mycobacterial heparin-binding hemagglutinin (HBHA), a protein that functions as an adhesin for epithelial cells. The structural gene was cloned from M. tuberculosis and bacillus Calmette-Guérin, and the sequence was found to be identical between the two species. The calculated Mr was smaller than the observed Mr when analyzed by SDS/PAGE. This difference can be attributed to the Lys/Pro-rich repeats that occur at the C-terminal end of the protein and to a putative carbohydrate moiety. Glycosylation of HBHA appears to protect the protein from proteolytic degradation, which results in the removal of the C-terminal Lys/Pro-rich region responsible for binding of HBHA to sulfated carbohydrates. Evidence suggests that glycosylation is also important for HBHA-mediated hemagglutination and for certain immunologic properties of the protein. Finally, the absence of a signal peptide in the coding region of HBHA raises the possibility that this protein is not secreted via the general secretion pathway.

Indexed as

Adhesins, BacterialAmino Acid SequenceBase SequenceCloning, MolecularDNA, BacterialEscherichia coliGenes, BacterialHemagglutininsLectinsMolecular Sequence DataMycobacterium bovisAdhesins, BacterialDNA, BacterialHemagglutininsheparin-binding hemagglutininLectins

Identifiers

PMID9770536
PMCPMC22881
OpenAlexW2101533192

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.