Parasite Immunology · 2003 · 45 citations · 14 references
Life SciencesImmunologyInfectious DiseasesEnzymologyMucosal ImmunologyProteomicsProteolytic EnzymesSheep Infectious DiseasesSheep ParasitologyVeterinary ImmunologyAspartic ProteasesDigestive ProteasesHaemonchus Contortus InfectionsIntegral Membrane ProteinsIntestinal Brush Border EnzymesParasitic ProteasesProtective Antigen IdentificationProtective Antigens
A novel pepsin-like aspartyl protease was identified as a component of Haemonchus galactose-containing glycoprotein (H-gal-GP), which is an integral membrane glycoprotein complex located on the intestinal cells of Haemonchus contortus, and a highly protective antigen for sheep. This molecule, designated HcPEP2, showed 50% sequence identity with a previously described aspartyl protease from H-gal-GP known as HcPEP1. Fractions of H-gal-GP, either containing both HcPEP1 and 2 or other lower molecular weight components of the complex, were evaluated as protective antigens in immunization - challenge trials in sheep. When separated from the rest of the complex by gel filtration in 8 m urea, the HcPEP1 and 2 fraction significantly reduced H. contortus egg counts by 48% and worm numbers by 36%, but the lower molecular weight components were not significantly protective. However, the HcPEP1 and 2 fraction did not protect if electro-eluted from SDS-dissociated H-gal-GP, nor did bacterially expressed recombinant HcPEP1, suggesting that conformational epitopes are important for inducing immunity.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations
David Longbottom, Diane Redmond, Mary E. Russell et al. · Molecular and Biochemical Parasitology · 1997 · 90 citations