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Vaccination of sheep with purified serine proteases from the secretory and excretory material of Lucilia cuprina larvae.
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Sheep were vaccinated with two purified serine proteases, LCT25a and LCT25b, isolated from the secretory and excretory material from first instar larvae of Lucilia cuprina. The immunization produced a strong antibody response to LCT25b and a weaker response to LCT25a as measured by ELISA. However,
Vaccination against Lucilia cuprina: the causative agent of sheep blowfly strike.
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The sheep blowfly, Lucilia cuprina, is responsible for over 80% of cases of blowfly strike in Australia and the losses in production and sheep deaths due to flystrike exceed $200 million per annum. Traditional methods of control are becoming less effective because of the blowfly's resistance to
Prospects for the control of sheep blowfly strike by vaccination.
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Research into vaccination against flystrike is aimed at either controlling the predisposing condition, fleece rot, or direct control of the fly maggots. A vaccine against the major bacterial species found in fleece rot lesions, Pseudomonas aeruginosa, is undergoing field trials and results suggest
Serine protease activity in excretory-secretory products of Oestrus ovis (Diptera: Oestridae) larvae.
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The sheep bot fly, Oestrus ovis, is a very common myiasis of nasal and sinus cavities of sheep and goats causing severe welfare and production implications. As the viability of O. ovis adult flies strictly depends on larval abilities to assimilate and to stock nutrients from the host, it was
Sheep plasma protease inhibitors influencing protease activity and growth of Lucilia cuprina larvae in vitro.
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The enzyme inhibitors alpha 2-macroglobulin (alpha 2M), anti-thrombin III (AT III) and alpha 1-proteinase inhibitor (alpha 1PI) were isolated from sheep plasma and tested for their ability to affect L. cuprina larval proteases and larval growth in vitro. Casein radial diffusion gels indicated that
Excretory/secretory chymotrypsin from Lucilia cuprina: purification, enzymatic specificity and amino acid sequence deduced from mRNA.
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Two chymotrypsin-like proteases were purified from the secretory and excretory material of first-instar larvae of Lucilia cuprina. The hydrolysis of N-succinyl-L-phenylalanine-nitroanilide was used to monitor the purification of these proteases which was achieved by affinity chromatography on
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