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      Secreted proteases from dermatophytes.

      Mycopathologia
      Animals, Exopeptidases, secretion, Humans, Keratins, metabolism, Metalloproteases, Microsporum, enzymology, pathogenicity, Serine Endopeptidases, Sulfites, Trichophyton, Virulence

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          Abstract

          Dermatophytes are highly specialized pathogenic fungi that exclusively infect the stratum corneum, nails or hair, and it is evident that secreted proteolytic activity is important for their virulence. Endo- and exoproteases-secreted by dermatophytes are similar to those of species of the genus Aspergillus. However, in contrast to Aspergillus spp., dermatophyte-secreted endoproteases are multiple and are members of two large protein families, the subtilisins (serine proteases) and the fungalysins (metalloproteases). In addition, dermatophytes excrete sulphite as a reducing agent. In the presence of sulphite, disulphide bounds of the keratin substrate are directly cleaved to cysteine and S-sulphocysteine, and reduced proteins become accessible for further digestion by various endo- and exoproteases secreted by the fungi. Sulphitolysis is likely to be an essential step in the digestion of compact keratinized tissues which precedes the action of all proteases.

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          Author and article information

          Journal
          18478360
          10.1007/s11046-008-9105-4

          Chemistry
          Animals,Exopeptidases,secretion,Humans,Keratins,metabolism,Metalloproteases,Microsporum,enzymology,pathogenicity,Serine Endopeptidases,Sulfites,Trichophyton,Virulence

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