Evidence map›Paper›PMID 9064359›Full record

ArticleThe Journal of experimental medicine1996

Identification of a heparin-binding hemagglutinin present in mycobacteria.

F D Menozzi, J H Rouse, M Alavi, M Laude-Sharp, J Muller, R Bischoff, M J Brennan, C Locht

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.

0numbers the graph read from it
0cells of the map it votes in
106citing papers in PubMed
2.1field-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

106 citing papers in PubMed, 277 citations in OpenAlex.

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  8. Dual oxidase 1 is dispensable duringFrontiers in immunology · 2023
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  10. Identification of theProceedings of the National Academy of Sciences of the United States of America · 2022
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  15. Article
  16. Review
  17. Effect ofEvidence-based complementary and alternative medicine : eCAM · 2020
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  18. Host Cell Targets of Released Lipid and Secreted Protein Effectors ofFrontiers in cellular and infection microbiology · 2020
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  19. Article
  20. Adhesion molecules facilitate host-pathogen interaction & mediateThe Indian journal of medical research · 2019
    Review

46 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

8 authors at 1 institution in 1 country.

F D MenozziLaboratoire de Microbiologie Genetique et Moléculare, Institut National de la Santé et de la Recherche Médicale U447, Institut Pasteur de Lille, France.
J H Rouse
M Alavi
M Laude-Sharp
J Muller
R Bischoff
M J Brennan
C Locht
Institut Pasteur · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Adherence to mammalian host tissues is an important virulence trait in microbial pathogenesis, yet little is known about the adherence mechanisms of mycobacteria. Here, we show that binding of mycobacteria to epithelial cells but not to macrophages can be specifically inhibited by sulfated carbohydrates. Using heparin-Sepharose chromatography, a 28-kD heparin-binding protein was purified from culture supernatants and cell extracts of Mycobacterium bovis and Mycobacterium tuberculosis. This protein, designated heparin-binding hemagglutinin (HBHA), promotes the agglutination of rabbit erythrocytes, which is specifically inhibited by sulfated carbohydrates. HBHA also induce mycobacterial aggregation, suggesting that it can mediate bacteria-bacteria interactions as well. Hemagglutination, mycobacterial aggregation, as well as attachment to epithelial cells are specifically inhibited in the presence of anti-HBHA antibodies. Immunoelectron microscopy using anti-HBHA monoclonal antibodies revealed that the protein is surface exposed, consistent with a role in adherence. Immunoblot analyses using antigen-specific antibodies indicated that HBHA is different from the fibronectin-binding proteins of the antigen 85 complex and p55, and comparison of the NH2-terminal amino acid sequence of purified HBHA with the protein sequence data bases did not reveal any significant similarity with other known proteins. Sera from tuberculosis patients but not from healthy individuals were found to recognize HBHA, indicating its immunogenicity in humans during mycobacterial infections. Identification of putative mycobacterial adhesins, such as the one described in this report, may provide the basis for the development of new therapeutic and prophylactic strategies against mycobacterial diseases.

Indexed as

AnimalsBacterial AdhesionCell AdhesionCell AggregationChickensEpithelial CellsEpitheliumHemagglutininsHeparinHumansLectinsMolecular WeightMycobacterium bovisMycobacterium tuberculosisRabbitsTuberculosisHemagglutininsHeparinheparin-binding hemagglutininLectins

Identifiers

PMID9064359
PMCPMC2192777
OpenAlexW2135661903

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.