Acasp, a gene encoding a cathepsin D-like aspartic protease from the hookworm Ancylostoma caninum.
Intestinal infection with the zoonotic hookworm Ancylostoma caninum can provoke human eosinophilic enteritis. A cDNA was isolated from A. caninum, using an oligonucleotide primer designed to hybridize to the region encoding the consensus, catalytic site residues D32TGSSNLW of aspartic proteases. This novel cDNA encoded an aspartic protease zymogen of 422 amino acids, exhibiting 47% identity to the lysosomal aspartic protease of Aedes aegypti, 46% identity to the aspartic protease of Schistosoma japonicum, and 48.5% to human cathepsin D. Its deduced structure differed from that of cathepsin D in the loop 2 "flap," which holds the substrate at the active site, and by the presence of a COOH-terminal extension of approximately 30 residues.
Harrop
S A
SA
Molecular Parasitology Unit, and Australian Centre for International & Tropical Health & Nutrition, Queensland Institute of Medical Research, Australia.
Prociv
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P
Brindley
P J
PJ
D000595:Amino Acid Sequence; D000722:Ancylostoma / Q000201:enzymology* / Q000235:genetics; D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000235:genetics*; D003001:Cloning, Molecular; D015801:Helminth Proteins; D006801:Humans; D008969:Molecular Sequence Data; D010802:Phylogeny; D016133:Polymerase Chain Reaction; D017386:Sequence Homology, Amino Acid
D015801:Helminth Proteins; C101887:Acasp1 protein, Ancylostoma caninum; D016282:Aspartic Acid Endopeptidases