Identification of the major soluble cuticular glycoprotein of lymphatic filarial nematode parasites (gp29) as a secretory homolog of glutathione peroxidase.
We have cloned and identified the major cuticular glycoprotein (gp29) of lymphatic filarial nematode parasites as a homolog of the antioxidant enzyme glutathione peroxidase. The derived amino acid sequence predicted a protein of 25.8 kDa, with an amino-terminal hydrophobic signal peptide and two sites for N-linked glycosylation, consistent with the documented properties of gp29. Transcription of a full-length cDNA in an SP65 vector and subsequent translation of the RNA in reticulocyte lysates in vitro generated a protein of 27 kDa, which was glycosylated upon the addition of pancreatic microsomal membranes. A postulated role for this secreted enzyme could be inhibition of the oxidative burst of leukocytes and neutralization of secondary products of lipid peroxidation, thus providing one explanation for the resistance of these parasites to immune effector mechanisms and their persistence in the mammalian host.
Cookson
E
E
Department of Biochemistry, Imperial College of Science, Technology and Medicine, London, United Kingdom.
Blaxter
M L
ML
Selkirk
M E
ME
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002009:Brugia / Q000201:enzymology* / Q000235:genetics; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D005979:Glutathione Peroxidase / Q000235:genetics*; D006023:Glycoproteins / Q000235:genetics; D015801:Helminth Proteins / Q000235:genetics*; D008969:Molecular Sequence Data; D014176:Protein Biosynthesis; D016415:Sequence Alignment; D014158:Transcription, Genetic
D006023:Glycoproteins; D015801:Helminth Proteins; D004247:DNA; D005979:Glutathione Peroxidase