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Fungal and Parasitic Infections

A 32-Kilodalton Hydrolase Plays an Important Role in Paracoccidioides brasiliensis Adherence to Host Cells and Influences Pathogenicity

Orville Hernández, Agostinho J. Almeida, Angel Gonzalez, Ana Maria Garcia, Diana Tamayo, Luz Elena Cano, Angela Restrepo, Juan G. McEwen
Orville Hernández
1Instituto de Biología, Universidad de Antioquia, Medellín, Colombia
2Cellular and Molecular Biology Unit, Corporación para Investigaciones Biológicas (CIB), Medellín, Colombia
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  • For correspondence: orvillehr@hotmail.com
Agostinho J. Almeida
3Life and Health Sciences Research Institute (ICVS), School of Health Sciences, University of Minho, Braga, Portugal
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Angel Gonzalez
4Medical and Experimental Mycology Group, Corporación para Investigaciones Biológicas (CIB), Medellín, Colombia
5Escuela de Microbiología, Universidad de Antioquia, Medellín, Colombia
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Ana Maria Garcia
2Cellular and Molecular Biology Unit, Corporación para Investigaciones Biológicas (CIB), Medellín, Colombia
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Diana Tamayo
2Cellular and Molecular Biology Unit, Corporación para Investigaciones Biológicas (CIB), Medellín, Colombia
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Luz Elena Cano
4Medical and Experimental Mycology Group, Corporación para Investigaciones Biológicas (CIB), Medellín, Colombia
5Escuela de Microbiología, Universidad de Antioquia, Medellín, Colombia
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Angela Restrepo
4Medical and Experimental Mycology Group, Corporación para Investigaciones Biológicas (CIB), Medellín, Colombia
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Juan G. McEwen
2Cellular and Molecular Biology Unit, Corporación para Investigaciones Biológicas (CIB), Medellín, Colombia
6Facultad de Medicina, Universidad de Antioquia, Medellín, Colombia
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DOI: 10.1128/IAI.00692-10
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ABSTRACT

One of the most crucial events during infection with the dimorphic fungus Paracoccidioides brasiliensis is adhesion to pulmonary epithelial cells, a pivotal step in the establishment of disease. In this study, we have evaluated the relevance of a 32-kDa protein, a putative adhesion member of the haloacid dehalogenase (HAD) superfamily of hydrolases, in the virulence of this fungus. Protein sequence analyses have supported the inclusion of PbHad32p as a hydrolase and have revealed a conserved protein only among fungal dimorphic and filamentous pathogens that are closely phylogenetically related. To evaluate its role during the host-pathogen interaction, we have generated mitotically stable P. brasiliensis HAD32 (PbHAD32) antisense RNA (aRNA) strains with consistently reduced gene expression. Knockdown of PbHAD32 did not alter cell vitality or viability but induced morphological alterations in yeast cells. Moreover, yeast cells with reduced PbHAD32 expression were significantly affected in their capacity to adhere to human epithelial cells and presented decreased virulence in a mouse model of infection. These data support the hypothesis that PbHad32p binds to extracellular matrix (ECM) proteins and modulates the initial immune response for evasion of host defenses. Our findings point to PbHAD32 as a novel virulence factor active during the initial interaction with host cells in P. brasiliensis.

  • Copyright © 2010 American Society for Microbiology
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A 32-Kilodalton Hydrolase Plays an Important Role in Paracoccidioides brasiliensis Adherence to Host Cells and Influences Pathogenicity
Orville Hernández, Agostinho J. Almeida, Angel Gonzalez, Ana Maria Garcia, Diana Tamayo, Luz Elena Cano, Angela Restrepo, Juan G. McEwen
Infection and Immunity Nov 2010, 78 (12) 5280-5286; DOI: 10.1128/IAI.00692-10

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A 32-Kilodalton Hydrolase Plays an Important Role in Paracoccidioides brasiliensis Adherence to Host Cells and Influences Pathogenicity
Orville Hernández, Agostinho J. Almeida, Angel Gonzalez, Ana Maria Garcia, Diana Tamayo, Luz Elena Cano, Angela Restrepo, Juan G. McEwen
Infection and Immunity Nov 2010, 78 (12) 5280-5286; DOI: 10.1128/IAI.00692-10
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KEYWORDS

Paracoccidioides
Paracoccidioidomycosis

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