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Characterization of a cDNA encoding a subtilisin-like serine protease (NC-p65) ofNeospora caninum

Authors
Journal
Molecular and Biochemical Parasitology
0166-6851
Publisher
Elsevier
Publication Date
Volume
103
Issue
2
Identifiers
DOI: 10.1016/s0166-6851(99)00127-9
Keywords
  • Neospora Caninum
  • Nc-P65
  • Subtilisin-Like Serine Protease
  • Subtilase
Disciplines
  • Biology

Abstract

Abstract The NC-p65 cDNA is the first protease sequence cloned and described for Neospora caninum. The full length cDNA was isolated by 5′- and 3′-rapid amplification of cDNA ends (RACE). NC-p65 was composed of 865 amino acids with a predicted signal sequence, a proposed pro-domain, and an internal region of conserved repeats. Analysis of the deduced amino acid sequence revealed that this protein had homology to the serine proteases of the subtilisin-like superfamily (subtilases) and had a predicted active site made up of the catalytic residues, Asp 253, His 309, and Ser 484. Antibodies to recombinant NC-p65 recognized multiple bands on Neospora lysate immunoblots, but most intensely stained a 65 kDa band. When N. caninum proteins were purified with affinity resins specific for NC-p65 and analyzed for enzyme activity, a single specific band of reaction was observed on gelatin-saturated zymograms.

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