Pharmacology and Therapeutics - Research Publications
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ItemVenomous injury surveillance in Brazil and Australia(University of Melbourne, Department of Pharmacology and Therapeutics, 2016-04-03)Reliable information of morbidity and mortality from venomous injuries are essential for effective state and national health policies for the prevention and treatment of this injury. Brazil and Australia are known for the numerous venomous animals that reside on these continents from snakes, scorpions to spiders. Nevertheless the burden of this injury is very different. Envenomation injury in Brazil is a notifiable event reported by the hospital. These notifications have demonstrated a burden of 206 per 100,000 people bitten or stung annually, whereas Australia demonstrates 36 per 100,000 hospitalisations per year attributed to a bite or sting. The overall health frameworks between the two countries are similar. Brazil has an established national health surveillance system, principles and guidelines to support the epidemiological understanding of injuries and accidents caused by envenomation, the logistical capacity to delivery timely medications and equipment and the education system to produce informed professionals. We will discuss the surveillance, health system framework to compare and contrast the two countries in order to identify areas of overlap and lessons learned between the two countries.
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ItemNo Preview AvailableMarasin Stoa Kipa training manual: Trainer of trainer manual(Oilsearch Limited, 2013-10-01)
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ItemNo Preview AvailableHospitalisation and deaths due to venomous bites and stings in Australia from 2000 to 2013(International society of toxinologists, 2015-09-28)
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ItemNo Preview AvailableDeath from venomous animals in Australia: not always in the bush(University of Melbourne, Department of Pharmacology and Therapeutics, 2015-09-03)
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ItemNo Preview AvailableOilsearch Limited community health village based treatment access program(Medicine for Malaria Venture, 2011-06-03)
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ItemNo Preview AvailableA malaria program response to an outbreak in a Southern Highlands village, Papua New Guinea(Australasian College of Tropical Medicine, 2011-01-16)A malaria program was set up in the Papuan village of Tugiri in 2005 after an initial prevalence survey indicated a malaria infection rate of 20%. The program's goal to reduce malaria transmission at Tugiri had been achieved, with a prevalence rate of 2% recorded in 2009. In March 2009 an outbreak was identified through the surveillance system set up at the village - an outbreak that was the result of a series of events which combined to complete the malaria transmission cycle. Three response stages were initiated to address the outbreak that included access to diagnosis and treatment, education for health staff and community, and environmental control measures. Continuing surveillance indicated that the outbreak, and the local transmission cycle, had been broken by June 2009.
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ItemProteomic and genomic characterisation of venom proteins from Oxyuranus species( 2005-06-30)The genus Oxyuranus includes three of the largest and most feared Australasian snakes, and are listed within the top ten of the world's most venomous snakes. This genus includes Oxyuranus microlepidotus (inland taipan), Oxyuranus scutellatus scutellatus (coastal taipan) and the subspecies Oxyuranus scutellatus canni (Papuan taipan). Despite comparative differences in the proportions of venom components the Oxyuranus species have been reported to be more closely related to each other than to those of any other large Australian elapid snakes. Nevertheless, differences in the clinical presentation of envenomed patients have been described between species. It has also been shown that the antivenom (produced from O. s. scutellatus) may not be as effective in bite victims of O. microlepidotus or O. s. canni compared to O. s. scutellatus. This project was a comparative study designed to substantially build upon previous research into the venom of Oxyuranus species. The objectives of this study were: firstly, to conduct a comparative study of the composition of venom proteins from the three Oxyuranus species; secondly to clone and characterise venom specific proteins. This study was primarily conducted utilising fundamental proteomic tools including chromatography, one- and two-dimensional gel electrophoresis (2DE) mass spectrometry and N-terminal sequence determination. The third objective was to use a cDNA expression library, constructed using mRNA from a venom gland of O. s. scutellatus, to screen with taipan antivenom in order to isolate nucleotide sequences important within the venom. The venoms from Oxyuranus showed remarkable complexity and stability. It was shown that the three Oxyuranus venoms share strong similarities in the protein patterning of major proteins. O. s. scutellatus and O. s. canni venoms exhibited identical protein patterning throughout electrophoretic, fractionation and immunobinding analysis. The venom similarities, together with previous comparative research using mitochondrial DNA sequencing and morphology studies indicated O. canni is not a subspecies but the same species of O. s. scutellatus. O. microlepidotus on the other hand, though sharing major proteins, revealed patterns distinctly different to O. s. scutellatus through electrophoretic and fractionation examinations. Immunobinding studies showed the major banding differences in O. microlepidotus were antigenic against taipan antivenom (CSL). These results also indicated that diet, feeding and habitat (captive/wild) do not play a major role in contributing to the venom compositions of the taipan, opposing literature stating the contrary in other species. Variation within the venom composition between the species may be due, instead, to the geographic distances and habitat pressures between the species. From these comparisons, an antigenic 300 kDa glycoprotein from O. s. scutellatus was identified using 15% SDS-PAGE and was isolated using size exclusion and affinity chromatography. This protein was comprised of a homo trimer, three subunits of 100kDa joined by disulphide bonds. N-terminal sequence shared homology to a previously identified serine protease. This protein cleaved chromogenic substrate S-2288 and Michaelis-Menten kinetics revealed this protein to undergo allosteric interactions. Results of inhibition profiles, pH optimum and kinetic studies confirmed this to be a trypsin-like serine protease. It was highly sensitive to benzamidine and PMSF and was inhibited only by high concentrations of alkylating and reducing agents NEM and iodoacetamide. Metal chelators 1,10-phenanthroline, EGTA and EDTA showed little inhibition; whereas SDS was the only reagent to completely prevent any activity. Based on this evidence it is proposed all three subunits are required for activity. This protease appeared to be present in the venoms of both O. microlepidotus and O. s. canni and may represent another coagulative enzyme within the venom. Sequencing studies elucidated the nucleotide sequences of a variety of clones from an O. s. scutellatus cDNA library. These clones, translated into full-length protein sequences, included homologous matches to characterised proteins including polymerases, carboxylases, dehydrogenases, Protein disulphide isomerases (PDI's), Heat shock proteins (HSP's) and myosin. Based on the sequences obtained, six PLA2 toxins, two post-synaptic toxins and the complete factor V component of a prothrombin activator (scutelarin) were proposed. This study represents the first report of full-length amino acid sequences of taipan venom proteins; previous studies have been conducted using isolated venom proteins that lack the nucleotide and transit peptide sequences. cDNA and deduced amino acid sequences were compared with those of other snake species. These comparisons conformed to the established primary structures found within the differing peptide classes and, within the putative pre-synaptic neurotoxins, conformed to the evolutionary outline suggested for these sequences.
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ItemThe composition and actions of Papua New Guinean snake venoms(Independent Publishing, 2004-05-01)Snake venoms are complex mixtures of bioactive agents with diverse pharmacological activities against a wide range of physiological targets. Many of these agents are complex chemicals which have toxic effects upon the cells and cellular mechanisms that they target, and in some snakes the toxicity is sufficient to be extremely harmful to man. Understanding the composition and activities of different snake venoms forearms clinicians with a knowledge of the underlying physiological changes responsible for clinical envenomation syndromes. In some cases this knowledge may enable presumptive identification of the biting species and early selection of the most appropriate antivenom.