Characterisation of an extracellular serine protease gene (nasp gene) from Dermatophilus congolensis.
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.
Garcia-Sanchez
Alfredo
A
Infectious Disease Unit, Medicine and Animal Health, University of Extremadura, Campus UEX, Avda. Universidad s/n, 10071 Caceres, Spain.
Cerrato
Rosario
R
Larrasa
Jose
J
Ambrose
Nicholas C
NC
Parra
Alberto
A
Alonso
Juan M
JM
Hermoso-de-Mendoza
Miguel
M
Rey
Joaquin M
JM
Mine
Madisa O
MO
Carnegie
Patrick R
PR
Ellis
Trevor M
TM
Masters
Anne M
AM
Pemberton
Alan D
AD
Hermoso-de-Mendoza
Javier
J
D000192:Actinomycetales / Q000737:chemistry / Q000201:enzymology / Q000235:genetics*; D000595:Amino Acid Sequence; D017931:DNA Primers; D004269:DNA, Bacterial / Q000302:isolation & purification; D005784:Gene Amplification; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000235:genetics* / Q000276:immunology
D017931:DNA Primers; D004269:DNA, Bacterial; D012697:Serine Endopeptidases