A PR-1-like Protein of Fusarium oxysporum Functions in Virulence on Mammalian Hosts

The pathogenesis-related PR-1-like protein family comprises secreted proteins from the animal, plant, and fungal kingdoms whose biological function remains poorly understood. Here we have characterized a PR-1-like protein, Fpr1, from Fusarium oxysporum, an ubiquitous fungal pathogen that causes vasc...

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Published inThe Journal of biological chemistry Vol. 287; no. 26; pp. 21970 - 21979
Main Authors Prados-Rosales, Rafael C., Roldán-Rodríguez, Raquel, Serena, Carolina, López-Berges, Manuel S., Guarro, Josep, Martínez-del-Pozo, Álvaro, Di Pietro, Antonio
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 22.06.2012
American Society for Biochemistry and Molecular Biology
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Summary:The pathogenesis-related PR-1-like protein family comprises secreted proteins from the animal, plant, and fungal kingdoms whose biological function remains poorly understood. Here we have characterized a PR-1-like protein, Fpr1, from Fusarium oxysporum, an ubiquitous fungal pathogen that causes vascular wilt disease on a wide range of plant species and can produce life-threatening infections in immunocompromised humans. Fpr1 is secreted and proteolytically processed by the fungus. The fpr1 gene is required for virulence in a disseminated immunodepressed mouse model, and its function depends on the integrity of the proposed active site of PR-1-like proteins. Fpr1 belongs to a gene family that has expanded in plant pathogenic Sordariomycetes. These results suggest that secreted PR-1-like proteins play important roles in fungal pathogenicity. Pathogenesis-related (PR-1-like) proteins are widely conserved in eukaryotes, but their biological function is unknown. Knockout or site-directed mutagenesis of fpr1 encoding a secreted PR-1-like protein in the fungal pathogen Fusarium oxysporum impairs virulence on mice. Secreted PR-1-like proteins are important for fungal infection of mammals. We show the first genetic evidence for a biological function of the predicted active site of PR-1-like proteins.
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Present address: Department of Microbiology and Immunology, Albert Einstein College of Medicine, Yeshiva University, Bronx, NY 10461.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M112.364034