Cuticular lipids of adults and puparia of the Australian sheep blowfly Lucilia cuprina (Wied.).

The biology and ecology of the Australian sheep blowfly, Lucilia cuprina (Wiedemann) – an update

Implications of insecticide resistance for the control of flystrike and lice on sheep

The Australian sheep blowfly (Lucilia cuprina) and the sheep body louse (Bovicola ovis) have both demonstrated their propensity to develop resistance to insecticides used for their control. Most populations of L. cuprina contain individuals resistant to organochlorines and organophosphates. Some are also resistant to benzoylphenyl ureas. Many populations of B. ovis are resistant to pyrethroid i...

Histone deacetylase enzymes as drug targets for the control of the sheep blowfly, Lucilia cuprina

The Australian sheep blowfly, Lucilia cuprina, is an ecto-parasite that causes significant economic losses in the sheep industry. Emerging resistance to insecticides used to protect sheep from this parasite is driving the search for new drugs that act via different mechanisms. Inhibitors of histone deacetylases (HDACs), enzymes essential for regulating eukaryotic gene transcription, are prospec...

Estimating population densities of the Australian sheep blowfly Lucilia cuprina (Wiedemann) (Diptera: Calliphoridae) from catches in wind-oriented traps

An analysis of 2-hourly catches of the blowfly, Lucilia cuprina, in 10 wind-oriented fly traps on 34 trapping days (06.00 – 18.00h) during the period November 1984 – May 1985 indicated that air temperature was the principal factor regulating the number of insects caught. Small but significant effects were associated with radiation, time of day and relative humidity; effects due to wind were not...

Purification, molecular cloning and heterologous expression of a glutathione S-transferase from the Australian sheep blowfly (Lucilia cuprina).

Three glutathione S-transferases from Lucilia cuprina (Australian sheep blowfly) pupae were purified by affinity chromatography and anion-exchange chromatography. One isoenzyme was composed of M(r)-24,800 subunits, and two isoenzymes had subunits of M(r) 23,900. The M(r)-23,900 subunits showed immunological identity and were immunologically distinct from the M(r)-24,800 subunits. All three enzy...