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Characterization, cloning and host-protective activity of a 30-kilodalton glycoprotein secreted by the parasitic stages of Trichostrongylus colubriformis.

作者信息

Savin K W, Dopheide T A, Frenkel M J, Wagland B M, Grant W N, Ward C W

机构信息

CSIRO Division of Biotechnology, Parkville, Australia.

出版信息

Mol Biochem Parasitol. 1990 Jun;41(2):167-76. doi: 10.1016/0166-6851(90)90179-p.

Abstract

The helminth Trichostrongylus colubriformis is a parasitic nematode infecting the small intestine of sheep. We report the isolation and characterization of a 30-kDa glycoprotein capable of partially protecting guinea-pigs against the parasite. This glycoprotein is secreted by the L4 and adult parasitic stages of the worm. The sequence of three separate cDNA clones predicts the polypeptide to be about 15 kDa, with four N-linked carbohydrate chains and an internal disulphide bond. The clones also indicate the existence of sequence variability in this antigen. Limited sequence homology to a porcine intestinal peptide suggests an influence on host gut physiology.

摘要

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