The malate synthase of <it>Paracoccidioides brasiliensis </it>is a linked surface protein that behaves as an anchorless adhesin

<p>Abstract</p> <p>Background</p> <p>The pathogenic fungus <it>Paracoccidioides brasiliensis </it>is the agent of paracoccidioidomycosis (PCM). This is a pulmonary mycosis acquired by inhalation of fungal airborne propagules that can disseminate to several o...

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Main Authors: Pereira Maristela, de Almeida Soares Célia, Lenzi Henrique, de Fátima da Silva Julhiany, Mendes-Giannini Maria, da Silva Neto Benedito
Format: Article
Language:English
Published: BMC 2009-12-01
Series:BMC Microbiology
Online Access:http://www.biomedcentral.com/1471-2180/9/272
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spelling doaj-669260d7aa304deca21492fdd2af333b2020-11-24T23:08:22ZengBMCBMC Microbiology1471-21802009-12-019127210.1186/1471-2180-9-272The malate synthase of <it>Paracoccidioides brasiliensis </it>is a linked surface protein that behaves as an anchorless adhesinPereira Maristelade Almeida Soares CéliaLenzi Henriquede Fátima da Silva JulhianyMendes-Giannini Mariada Silva Neto Benedito<p>Abstract</p> <p>Background</p> <p>The pathogenic fungus <it>Paracoccidioides brasiliensis </it>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, <it>P. brasiliensis </it>may use the glyoxylate cycle for intracellular survival.</p> <p>Results</p> <p>Here, we provide evidence that the malate synthase of <it>P. brasiliensis </it>(<it>Pb</it>MLS) is located on the fungal cell surface, and is secreted. <it>Pb</it>MLS was overexpressed in <it>Escherichia coli</it>, and polyclonal antibody was obtained against this protein. By using Confocal Laser Scanning Microscopy, <it>Pb</it>MLS was detected in the cytoplasm and in the cell wall of the mother, but mainly of budding cells of the <it>P. brasiliensis </it>yeast phase. <it>Pb</it>MLSr and its respective polyclonal antibody produced against this protein inhibited the interaction of <it>P. brasiliensis </it>with <it>in vitro </it>cultured epithelial cells A549.</p> <p>Conclusion</p> <p>These observations indicated that cell wall-associated <it>Pb</it>MLS 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.</p> http://www.biomedcentral.com/1471-2180/9/272
collection DOAJ
language English
format Article
sources DOAJ
author Pereira Maristela
de Almeida Soares Célia
Lenzi Henrique
de Fátima da Silva Julhiany
Mendes-Giannini Maria
da Silva Neto Benedito
spellingShingle Pereira Maristela
de Almeida Soares Célia
Lenzi Henrique
de Fátima da Silva Julhiany
Mendes-Giannini Maria
da Silva Neto Benedito
The malate synthase of <it>Paracoccidioides brasiliensis </it>is a linked surface protein that behaves as an anchorless adhesin
BMC Microbiology
author_facet Pereira Maristela
de Almeida Soares Célia
Lenzi Henrique
de Fátima da Silva Julhiany
Mendes-Giannini Maria
da Silva Neto Benedito
author_sort Pereira Maristela
title The malate synthase of <it>Paracoccidioides brasiliensis </it>is a linked surface protein that behaves as an anchorless adhesin
title_short The malate synthase of <it>Paracoccidioides brasiliensis </it>is a linked surface protein that behaves as an anchorless adhesin
title_full The malate synthase of <it>Paracoccidioides brasiliensis </it>is a linked surface protein that behaves as an anchorless adhesin
title_fullStr The malate synthase of <it>Paracoccidioides brasiliensis </it>is a linked surface protein that behaves as an anchorless adhesin
title_full_unstemmed The malate synthase of <it>Paracoccidioides brasiliensis </it>is a linked surface protein that behaves as an anchorless adhesin
title_sort malate synthase of <it>paracoccidioides brasiliensis </it>is a linked surface protein that behaves as an anchorless adhesin
publisher BMC
series BMC Microbiology
issn 1471-2180
publishDate 2009-12-01
description <p>Abstract</p> <p>Background</p> <p>The pathogenic fungus <it>Paracoccidioides brasiliensis </it>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, <it>P. brasiliensis </it>may use the glyoxylate cycle for intracellular survival.</p> <p>Results</p> <p>Here, we provide evidence that the malate synthase of <it>P. brasiliensis </it>(<it>Pb</it>MLS) is located on the fungal cell surface, and is secreted. <it>Pb</it>MLS was overexpressed in <it>Escherichia coli</it>, and polyclonal antibody was obtained against this protein. By using Confocal Laser Scanning Microscopy, <it>Pb</it>MLS was detected in the cytoplasm and in the cell wall of the mother, but mainly of budding cells of the <it>P. brasiliensis </it>yeast phase. <it>Pb</it>MLSr and its respective polyclonal antibody produced against this protein inhibited the interaction of <it>P. brasiliensis </it>with <it>in vitro </it>cultured epithelial cells A549.</p> <p>Conclusion</p> <p>These observations indicated that cell wall-associated <it>Pb</it>MLS 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.</p>
url http://www.biomedcentral.com/1471-2180/9/272
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