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http://purl.uniprot.org/citations/14766908http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14766908http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14766908http://www.w3.org/2000/01/rdf-schema#comment"Dermatophytes are human and animal pathogenic fungi which cause cutaneous infections and grow exclusively in the stratum corneum, nails and hair. In a culture medium containing soy proteins as sole nitrogen source a substantial proteolytic activity was secreted by Trichophyton rubrum, Trichophyton mentagrophytes and Microsporum canis. This proteolytic activity was 55-75 % inhibited by o-phenanthroline, attesting that metalloproteases were secreted by all three species. Using a consensus probe constructed on previously characterized genes encoding metalloproteases (MEP) of the M36 fungalysin family in Aspergillus fumigatus, Aspergillus oryzae and M. canis, a five-member MEP family was isolated from genomic libraries of T. rubrum, T. mentagrophytes and M. canis. A phylogenetic analysis of genomic and protein sequences revealed a robust tree consisting of five main clades, each of them including a MEP sequence type from each dermatophyte species. Each MEP type was remarkably conserved across species (72-97 % amino acid sequence identity). The tree topology clearly indicated that the multiplication of MEP genes in dermatophytes occurred prior to species divergence. In culture medium containing soy proteins as a sole nitrogen source secreted Meps accounted for 19-36 % of total secreted protein extracts; characterization of protein bands by proteolysis and mass spectrometry revealed that the three dermatophyte species secreted two Meps (Mep3 and Mep4) encoded by orthologous genes."xsd:string
http://purl.uniprot.org/citations/14766908http://purl.org/dc/terms/identifier"doi:10.1099/mic.0.26690-0"xsd:string
http://purl.uniprot.org/citations/14766908http://purl.org/dc/terms/identifier"doi:10.1099/mic.0.26690-0"xsd:string
http://purl.uniprot.org/citations/14766908http://purl.uniprot.org/core/author"Barblan J."xsd:string
http://purl.uniprot.org/citations/14766908http://purl.uniprot.org/core/author"Barblan J."xsd:string
http://purl.uniprot.org/citations/14766908http://purl.uniprot.org/core/author"Quadroni M."xsd:string
http://purl.uniprot.org/citations/14766908http://purl.uniprot.org/core/author"Quadroni M."xsd:string
http://purl.uniprot.org/citations/14766908http://purl.uniprot.org/core/author"Monod M."xsd:string
http://purl.uniprot.org/citations/14766908http://purl.uniprot.org/core/author"Monod M."xsd:string
http://purl.uniprot.org/citations/14766908http://purl.uniprot.org/core/author"Mignon B."xsd:string
http://purl.uniprot.org/citations/14766908http://purl.uniprot.org/core/author"Mignon B."xsd:string
http://purl.uniprot.org/citations/14766908http://purl.uniprot.org/core/author"Lechenne B."xsd:string
http://purl.uniprot.org/citations/14766908http://purl.uniprot.org/core/author"Lechenne B."xsd:string
http://purl.uniprot.org/citations/14766908http://purl.uniprot.org/core/author"Jousson O."xsd:string
http://purl.uniprot.org/citations/14766908http://purl.uniprot.org/core/author"Jousson O."xsd:string
http://purl.uniprot.org/citations/14766908http://purl.uniprot.org/core/author"Bontems O."xsd:string
http://purl.uniprot.org/citations/14766908http://purl.uniprot.org/core/author"Bontems O."xsd:string
http://purl.uniprot.org/citations/14766908http://purl.uniprot.org/core/author"Capoccia S."xsd:string
http://purl.uniprot.org/citations/14766908http://purl.uniprot.org/core/author"Capoccia S."xsd:string
http://purl.uniprot.org/citations/14766908http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14766908http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14766908http://purl.uniprot.org/core/name"Microbiology"xsd:string
http://purl.uniprot.org/citations/14766908http://purl.uniprot.org/core/name"Microbiology"xsd:string