Characterisation of an extracellular serine protease gene (nasp gene) from Dermatophilus congolensis.

نویسندگان

  • Alfredo Garcia-Sanchez
  • Rosario Cerrato
  • Jose Larrasa
  • Nicholas C Ambrose
  • Alberto Parra
  • Juan M Alonso
  • Miguel Hermoso-de-Mendoza
  • Joaquin M Rey
  • Madisa O Mine
  • Patrick R Carnegie
  • Trevor M Ellis
  • Anne M Masters
  • Alan D Pemberton
  • Javier Hermoso-de-Mendoza
چکیده

A partial amino acid sequence of a serine protease from Dermatophilus congolensis allowed the design of oligonucleotide primers that were complemented with additional ones from previously published partial sequences of the gene encoding the enzyme. The polymerase chain reaction (PCR), using combinations of specific and degenerate oligonucleotide primers, allowed the amplification of a 1738-bp internal fragment of the gene, which was finally characterised by inverse PCR as the first full-length sequenced serine protease gene (nasp) from Dermatophilus congolensis. The deduced amino acid sequence of this enzyme, probably involved in the pathogenesis of dermatophilosis, links it to the subtilisin family of proteases.

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عنوان ژورنال:
  • FEMS microbiology letters

دوره 231 1  شماره 

صفحات  -

تاریخ انتشار 2004