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Developmentally regulated secretion of cathepsin L-like cysteine proteases by Haemonchus contortus.
J Parasitol. 1995 Aug; 81(4):505-12.JP

Abstract

Cysteine protease activity was present in media collected after 24 hr in vitro culture of adult Haemonchus contortus. The released cysteine protease hydrolyzed the fluorogenic 7-amino-4-trifluoromethyl coumarin (AFC)-substituted synthetic peptides Z-phe-arg-AFC and Z-ala-arg-arg-AFC, but not Z-arg-arg-AFC or Z-arg-AFC, characterizing this activity as cathepsin L-like. Within the parasite, cysteine protease activity was highest in extracts of intestinal tissue. Secreted cysteine protease inhibited the clotting of sheep blood and hydrolyzed hemoglobin, fibrinogen, collagen, and IgG; the IgG hydrolysis site was within the hinge region. Four proteases with M(r) values of 30, 34, 37, and 41 kDa were identified with biotinylated-phenylalanine-arginine-fluoromethyl ketone, a specific probe that binds to active cysteine proteases. Adult parasites cultivated in the presence of 0.1 mM levamisole released 50% less protease activity compared to control cultures; in the presence of rafoxanide (0.1 mM), protease was not detected. Cathepsin L-like cysteine protease activity was released also by L4, but not the L3 larval stage. The active and developmentally regulated release of cysteine proteases by H. contortus may have a critical function in worm nutrition, immune evasion, or both.

Authors+Show Affiliations

Rhoads ML
Livestock and Poultry Sciences Institute, United States Department of Agriculture, Beltsville, Maryland 20705, USA.
Fetterer RH
No affiliation info available

MeSH

Amino Acid SequenceAnimalsAnthelminticsBlood CoagulationCathepsin LCathepsinsCysteine EndopeptidasesElectrophoresis, Polyacrylamide GelEndopeptidasesFluorescent DyesHaemonchusHydrolysisLarvaMolecular Sequence DataProteinsSheepSubstrate Specificity

Pub Type(s)

Journal Article

Language

eng

PubMed ID

7623189

Citation

Rhoads, M L., and R H. Fetterer. "Developmentally Regulated Secretion of Cathepsin L-like Cysteine Proteases By Haemonchus Contortus." The Journal of Parasitology, vol. 81, no. 4, 1995, pp. 505-12.
Rhoads ML, Fetterer RH. Developmentally regulated secretion of cathepsin L-like cysteine proteases by Haemonchus contortus. J Parasitol. 1995;81(4):505-12.
Rhoads, M. L., & Fetterer, R. H. (1995). Developmentally regulated secretion of cathepsin L-like cysteine proteases by Haemonchus contortus. The Journal of Parasitology, 81(4), 505-12.
Rhoads ML, Fetterer RH. Developmentally Regulated Secretion of Cathepsin L-like Cysteine Proteases By Haemonchus Contortus. J Parasitol. 1995;81(4):505-12. PubMed PMID: 7623189.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Developmentally regulated secretion of cathepsin L-like cysteine proteases by Haemonchus contortus. AU - Rhoads,M L, AU - Fetterer,R H, PY - 1995/8/1/pubmed PY - 1995/8/1/medline PY - 1995/8/1/entrez SP - 505 EP - 12 JF - The Journal of parasitology JO - J Parasitol VL - 81 IS - 4 N2 - Cysteine protease activity was present in media collected after 24 hr in vitro culture of adult Haemonchus contortus. The released cysteine protease hydrolyzed the fluorogenic 7-amino-4-trifluoromethyl coumarin (AFC)-substituted synthetic peptides Z-phe-arg-AFC and Z-ala-arg-arg-AFC, but not Z-arg-arg-AFC or Z-arg-AFC, characterizing this activity as cathepsin L-like. Within the parasite, cysteine protease activity was highest in extracts of intestinal tissue. Secreted cysteine protease inhibited the clotting of sheep blood and hydrolyzed hemoglobin, fibrinogen, collagen, and IgG; the IgG hydrolysis site was within the hinge region. Four proteases with M(r) values of 30, 34, 37, and 41 kDa were identified with biotinylated-phenylalanine-arginine-fluoromethyl ketone, a specific probe that binds to active cysteine proteases. Adult parasites cultivated in the presence of 0.1 mM levamisole released 50% less protease activity compared to control cultures; in the presence of rafoxanide (0.1 mM), protease was not detected. Cathepsin L-like cysteine protease activity was released also by L4, but not the L3 larval stage. The active and developmentally regulated release of cysteine proteases by H. contortus may have a critical function in worm nutrition, immune evasion, or both. SN - 0022-3395 UR - https://www.unboundmedicine.com/medline/citation/7623189/Developmentally_regulated_secretion_of_cathepsin_L_like_cysteine_proteases_by_Haemonchus_contortus_ DB - PRIME DP - Unbound Medicine ER -