Evidence map›Paper›PMID 20034376›Full record

ArticleBMC microbiology2009

The malate synthase of Paracoccidioides brasiliensis is a linked surface protein that behaves as an anchorless adhesin.

Benedito Rodrigues da Silva Neto, Julhiany de Fátima da Silva, Maria José Soares Mendes-Giannini, Henrique Leonel Lenzi, Célia Maria de Almeida Soares, Maristela Pereira

Open access · goldAbstract read
In one paragraph

Article in BMC microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.2field-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

24 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
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  4. In Vitro and In Vivo Effect of Peptides Derived from 14-3-3Journal of fungi (Basel, Switzerland) · 2021
    Article
  5. Review
  6. Mediators of inflammation · 2017
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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 3 institutions in 1 country.

Benedito Rodrigues da Silva NetoLaboratório de Biologia Molecular, Departamento de Bioquímica e Biologia Molecular, Instituto de Ciências Biológicas, Universidade Federal de Goiás, 74001-970 Goiânia, GO, Brazil.
Julhiany de Fátima da Silva
Maria José Soares Mendes-Giannini
Henrique Leonel Lenzi
Célia Maria de Almeida Soares
Maristela Pereira
Universidade Federal de Goiás · BRUniversidade Estadual Paulista (Unesp) · BRFundação Oswaldo Cruz · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe pathogenic fungus Paracoccidioides brasiliensis is the agent of paracoccidioidomycosis (PCM). This is a pulmonary mycosis acquired by inhalation of fungal airborne propagules that can disseminate to several organs and tissues leading to a severe form of the disease. Adhesion and invasion to host cells are essential steps involved in the internalization and dissemination of pathogens. Inside the host, P. brasiliensis may use the glyoxylate cycle for intracellular survival.

resultsHere, we provide evidence that the malate synthase of P. brasiliensis (PbMLS) is located on the fungal cell surface, and is secreted. PbMLS was overexpressed in Escherichia coli, and polyclonal antibody was obtained against this protein. By using Confocal Laser Scanning Microscopy, PbMLS was detected in the cytoplasm and in the cell wall of the mother, but mainly of budding cells of the P. brasiliensis yeast phase. PbMLSr and its respective polyclonal antibody produced against this protein inhibited the interaction of P. brasiliensis with in vitro cultured epithelial cells A549.

conclusionThese observations indicated that cell wall-associated PbMLS could be mediating the binding of fungal cells to the host, thus contributing to the adhesion of fungus to host tissues and to the dissemination of infection, behaving as an anchorless adhesin.

Indexed as

Antibodies, FungalBiotinylationCell LineCell WallCloning, MolecularEscherichia coliExtracellular Matrix ProteinsFungal ProteinsHumansMalate SynthaseMicroscopy, ConfocalParacoccidioidesProtein BindingRecombinant ProteinsAntibodies, FungalExtracellular Matrix ProteinsFungal ProteinsMalate SynthaseRecombinant Proteins

Identifiers

PMID20034376
PMCPMC2807876
OpenAlexW2063383030

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.