Evidence map›Paper›PMID 12438366›Full record

ArticleInfection and immunity2002

Purification and partial characterization of a 32-kilodalton sialic acid-specific lectin from Aspergillus fumigatus.

Guy Tronchin, Karine Esnault, Myriam Sanchez, Gerald Larcher, Agnes Marot-Leblond, Jean-Philippe Bouchara

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In one paragraph

Article in Infection and immunity, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

12 citing papers in PubMed, 59 citations in OpenAlex.

  1. Review
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  6. Opportunistic invasive fungal pathogen Macrophomina phaseolina prognosis from immunocompromised humans to potential mitogenic RBL with an exceptional and novel antitumor and cytotoxic effect.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2012
    Review
  7. Article
  8. Article
  9. Article
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  11. Article
  12. Lectin activity in mycelial extracts of Fusarium species.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]
    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

6 authors at 1 institution in 1 country.

Guy TronchinGroupe d'Etude des Interactions Hôte-Parasite, UPRES EA 3142, Laboratoire de Parasitologie-Mycologie, Centre Hospitalier Universitaire, Angers, France. guy.tronchin@univ-angers.fr
Karine Esnault
Myriam Sanchez
Gerald Larcher
Agnes Marot-Leblond
Jean-Philippe Bouchara
Université d'Angers · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Adherence of the opportunistic fungus Aspergillus fumigatus to the extracellular matrix components is considered a crucial step in the establishment of the infection. Given the high carbohydrate content of these glycoproteins and the role of carbohydrate-protein interactions in numerous adherence processes, the presence of a lectin in A. fumigatus was investigated. Different fungal extracts obtained by sonication or grinding in liquid nitrogen from resting or swollen conidia, as well as from germ tubes and mycelium, were tested by hemagglutination assays using rabbit erythrocytes. A lectin activity was recovered in all the extracts tested. However, sonication of resting conidia resulted in the highest specific activity. Purification of the lectin was achieved by gel filtration followed by ion-exchange and hydrophobic-interaction chromatographies. Analysis of the purified lectin by sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed an apparent molecular mass of 32 kDa, which is similar to that of the alkaline protease already identified from different strains of A. fumigatus. However, as evidenced by the use of an alkaline protease-deficient mutant, the two activities were supported by distinct proteins. In addition, hemagglutination inhibition experiments using different saccharides and glycoproteins demonstrated the specificity of the lectin for sialic acid residues. Together these results suggest that this lectin may contribute to the attachment of conidia to the extracellular matrix components through the recognition of the numerous terminal sialic acid residues of their carbohydrate chains.

Indexed as

AnimalsAspergillus fumigatusGlycoconjugatesHemagglutination Inhibition TestsHemagglutination TestsLectinsN-Acetylneuraminic AcidRabbitsSubstrate SpecificityGlycoconjugatesLectinsN-Acetylneuraminic Acid

Identifiers

PMID12438366
PMCPMC133100
OpenAlexW2123554423

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.