Genomic and Proteomic Dissection of the Ubiquitous Plant Pathogen, <i>Armillaria mellea</i>: Toward a New Infection Model System

Armillaria mellea is a major plant pathogen. Yet, no large-scale “-omics” data are available to enable new studies, and limited experimental models are available to investigate basidiomycete pathogenicity. Here we reveal that the <i>A. mellea</i> genome comprises 58.35 Mb, contains 14473 gene models, of average length 1575 bp (4.72 introns/gene). Tandem mass spectrometry identified 921 mycelial (<i>n</i> = 629 unique) and secreted (<i>n</i> = 183 unique) proteins. Almost 100 mycelial proteins were either species-specific or previously unidentified at the protein level. A number of proteins (<i>n</i> = 111) was detected in both mycelia and culture supernatant extracts. Signal sequence occurrence was 4-fold greater for secreted (50.2%) compared to mycelial (12%) proteins. Analyses revealed a rich reservoir of carbohydrate degrading enzymes, laccases, and lignin peroxidases in the <i>A. mellea</i> proteome, reminiscent of both basidiomycete and ascomycete glycodegradative arsenals. We discovered that <i>A. mellea</i> exhibits a specific killing effect against Candida albicans during coculture. Proteomic investigation of this interaction revealed the unique expression of defensive and potentially offensive <i>A. mellea</i> proteins (<i>n</i> = 30). Overall, our data reveal new insights into the origin of basidiomycete virulence and we present a new model system for further studies aimed at deciphering fungal pathogenic mechanisms

Genomic and Proteomic Dissection of the Ubiquitous Plant Pathogen, <i>Armillaria mellea</i>: Toward a New Infection Model System

Armillaria mellea is a major plant pathogen. Yet, no large-scale “-omics” data are available to enable new studies, and limited experimental models are available to investigate basidiomycete pathogenicity. Here we reveal that the <i>A. mellea</i> genome comprises 58.35 Mb, contains 14473 gene models, of average length 1575 bp (4.72 introns/gene). Tandem mass spectrometry identified 921 mycelial (<i>n</i> = 629 unique) and secreted (<i>n</i> = 183 unique) proteins. Almost 100 mycelial proteins were either species-specific or previously unidentified at the protein level. A number of proteins (<i>n</i> = 111) was detected in both mycelia and culture supernatant extracts. Signal sequence occurrence was 4-fold greater for secreted (50.2%) compared to mycelial (12%) proteins. Analyses revealed a rich reservoir of carbohydrate degrading enzymes, laccases, and lignin peroxidases in the <i>A. mellea</i> proteome, reminiscent of both basidiomycete and ascomycete glycodegradative arsenals. We discovered that <i>A. mellea</i> exhibits a specific killing effect against Candida albicans during coculture. Proteomic investigation of this interaction revealed the unique expression of defensive and potentially offensive <i>A. mellea</i> proteins (<i>n</i> = 30). Overall, our data reveal new insights into the origin of basidiomycete virulence and we present a new model system for further studies aimed at deciphering fungal pathogenic mechanisms

Genomic and Proteomic Dissection of the Ubiquitous Plant Pathogen, <i>Armillaria mellea</i>: Toward a New Infection Model System

Armillaria mellea is a major plant pathogen. Yet, no large-scale “-omics” data are available to enable new studies, and limited experimental models are available to investigate basidiomycete pathogenicity. Here we reveal that the <i>A. mellea</i> genome comprises 58.35 Mb, contains 14473 gene models, of average length 1575 bp (4.72 introns/gene). Tandem mass spectrometry identified 921 mycelial (<i>n</i> = 629 unique) and secreted (<i>n</i> = 183 unique) proteins. Almost 100 mycelial proteins were either species-specific or previously unidentified at the protein level. A number of proteins (<i>n</i> = 111) was detected in both mycelia and culture supernatant extracts. Signal sequence occurrence was 4-fold greater for secreted (50.2%) compared to mycelial (12%) proteins. Analyses revealed a rich reservoir of carbohydrate degrading enzymes, laccases, and lignin peroxidases in the <i>A. mellea</i> proteome, reminiscent of both basidiomycete and ascomycete glycodegradative arsenals. We discovered that <i>A. mellea</i> exhibits a specific killing effect against Candida albicans during coculture. Proteomic investigation of this interaction revealed the unique expression of defensive and potentially offensive <i>A. mellea</i> proteins (<i>n</i> = 30). Overall, our data reveal new insights into the origin of basidiomycete virulence and we present a new model system for further studies aimed at deciphering fungal pathogenic mechanisms